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Enzymes | Biology for All | FuseSchool
 
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Enzymes are really important proteins, that speed up the rates of reactions such as in photosynthesis, respiration and protein synthesis. The enzymes and substrates are always moving, and occasionally they collide at the right speed and orientation so that the substrate fits into the enzyme at the active site. Collision theory dictates that collisions must occur with sufficient energy and in a specific orientation for a reaction to occur. Enzymes are specialised; their active site matches the shape of the specific substrate that they react with. The enzyme and the substrate fit together using a lock and key mechanism. Once the substrate is in the active site, the reaction takes place. The required product is produced and the enzyme releases itself and carries on moving around. The enzyme could be protease, which breaks down proteins into amino acids. Or carbohydrase which breaks down carbohydrates into glucose. Or lipase which breaks down fats into fatty acids and glycerols. Hydrogen peroxide is often formed as a result of reactions in cells, and if it is left to build up it is harmful. Luckily, we have catalase enzymes that are really fast. They break the hydrogen peroxide down into the harmless water and oxygen. Equally, enzymes can help build up molecules like this… but the process is still exactly the same. Whilst enzymes do fantastic things, they are sensitive. Each enzyme has optimum conditions under which it works best. Firstly, there needs to be enough substrate around - they need a high enough substrate concentration for the reaction that they catalyse. If there is too little substrate, then the rate of reaction is slowed. Sometimes, if there is too much product around then the reaction slows because the enzymes and substrates have less chance of bumping into each other. So the product needs to be removed for a higher rate of reaction. Enzymes also have optimum pH and temperature conditions. Up to a point, an increase in temperature causes increased rate of reaction because there is more heat energy. More energy means more collisions. However, above a certain temperature the rate drops off due to denaturing. We will look at the effect of pH and temperature on enzymes in our video ‘Denaturation of Enzymes’. The pH and temperature optimum conditions are specific to the conditions in which they work in; an enzyme that works in the stomach for example would have a more acidic optimum pH. And of course, there need to be enough enzymes around for the rate of reaction to be optimised. So we know that enzymes and substrates fit together at the active site and form a ‘lock and key’ mechanism. The enzyme then releases the product and can be reused again. They are sensitive to temperature and pH, and there needs to be sufficient enzyme and substrate concentrations for reactions to occur. Enzymes not only control all kinds of reactions such as in photosynthesis, respiration, digestion and protein synthesis, but we also make use of them in day to day life. Protease and lipase enzymes are used in biological washing powders to remove proteins and fats from stains in our clothes. We also use enzymes in our food and drink industries; pectinase is used to break down the cells in fruit when making fruit juice so that more juice is released. SUBSCRIBE to the FuseSchool YouTube channel for many more educational videos. Our teachers and animators come together to make fun & easy-to-understand videos in Chemistry, Biology, Physics, Maths & ICT. VISIT us at www.fuseschool.org, where all of our videos are carefully organised into topics and specific orders, and to see what else we have on offer. Comment, like and share with other learners. You can both ask and answer questions, and teachers will get back to you. These videos can be used in a flipped classroom model or as a revision aid. Find all of our Chemistry videos here: https://www.youtube.com/watch?v=cRnpKjHpFyg&list=PLW0gavSzhMlReKGMVfUt6YuNQsO0bqSMV Find all of our Biology videos here: https://www.youtube.com/watch?v=tjkHzEVcyrE&list=PLW0gavSzhMlQYSpKryVcEr3ERup5SxHl0 Find all of our Maths videos here: https://www.youtube.com/watch?v=hJq_cdz_L00&list=PLW0gavSzhMlTyWKCgW1616v3fIywogoZQ Twitter: https://twitter.com/fuseSchool Access a deeper Learning Experience in the FuseSchool platform and app: www.fuseschool.org Follow us: http://www.youtube.com/fuseschool Friend us: http://www.facebook.com/fuseschool This Open Educational Resource is free of charge, under a Creative Commons License: Attribution-NonCommercial CC BY-NC ( View License Deed: http://creativecommons.org/licenses/by-nc/4.0/ ). You are allowed to download the video for nonprofit, educational use. If you would like to modify the video, please contact us: [email protected]
Function of Enzymes: Substrate, Active Site & Activation Energy
 
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Visit Study.com for thousands more videos like this one. You'll get full access to our interactive quizzes and transcripts and can find out how to use our videos to earn real college credit. YouTube hosts only the first few lessons in each course. The rest are at Study.com. Take the next step in your educational future and graduate with less debt and in less time.
Views: 120172 Study.com
Enzymes and Substrates
 
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a thingy about enzymes and stuff
Views: 20297 lucyshackell1
Enzyme substrate complex
 
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This enzymology video is about the enzyme substrate complex. http://shomusbiology.com/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching This video explains three important mechanisms by which an enzyme catalyses reactions. In biochemistry, a substrate is a molecule upon which an enzyme acts. Enzymes catalyze chemical reactions involving the substrate(s). In the case of a single substrate, the substrate bonds with the enzyme active site, and an enzyme-substrate complex is formed. The substrate is transformed into one or more products, which are then released from the active site. The active site is now free to accept another substrate molecule. In the case of more than one substrate, these may bind in a particular order to the active site, before reacting together to produce products. A substrate is called 'chromogenic', if it gives rise to a colored product when acted on by an enzyme. For example, curd formation (rennet coagulation) is a reaction that occurs upon adding the enzyme rennin to milk. In this reaction, the substrate is a milk protein (e.g., casein) and the enzyme is rennin. The products are two polypeptides that have been formed by the cleavage of the larger peptide substrate. Another example is the chemical decomposition of hydrogen peroxide carried out by the enzyme catalase. As enzymes are catalysts, they are not changed by the reactions they carry out. The substrate(s), however, is/are converted to product(s). Here, hydrogen peroxide is converted to water and oxygen gas. E + S ⇌ ES → EP ⇌ E + P where E = enzyme, S = substrate(s), P = product(s). While the first (binding) and third (unbinding) steps are, in general, reversible, the middle step may be irreversible (as in the rennin and catalase reactions just mentioned) or reversible (e.g., many reactions in the glycolysis metabolic pathway). By increasing the substrate concentration, the rate of reaction will increase due to the likelihood that the number of enzyme-substrate complexes will increase; this occurs until the enzyme concentration becomes the limiting factor. It is important to note that the substrates that a given amino acid in vitro may not necessarily reflect the physiological, endogenous substrates of the enzyme in vivo. That is to say that enzymes do not necessarily perform all the reactions in the body that may be possible in the laboratory. For example, while fatty acid amide hydrolase (FAAH) can hydrolyze the endocannabinoids 2-arachidonoylglycerol (2-AG) and anandamide at comparable rates in vitro, genetic or pharmacological disruption of FAAH elevates anandamide but not 2-AG, suggesting that 2-AG is not an endogenous, in vivo substrate for FAAH.[1] In another example, the N-acyl taurines (NATs) are observed to increase dramatically in FAAH-disrupted animals, but are actually poor in vitro FAAH substrates.[2] Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page
Views: 13455 Shomu's Biology
Enzymes (Updated)
 
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The Amoeba Sisters explain enzymes and how they interact with their substrates. Vocabulary covered includes active site, induced fit, coenzyme, and cofactor. Also the importance of ideal pH and temperatures for enzymes are discussed. This video has a handout here: http://www.amoebasisters.com/handouts.html Support us on Patreon! http://www.patreon.com/amoebasisters Our FREE resources: GIFs: http://www.amoebasisters.com/gifs.html Handouts: http://www.amoebasisters.com/handouts.html Comics: http://www.amoebasisters.com/parameciumparlorcomics Connect with us! Website: http://www.AmoebaSisters.com Twitter: http://www.twitter.com/AmoebaSisters Facebook: http://www.facebook.com/AmoebaSisters Tumblr: http://www.amoebasisters.tumblr.com Pinterest: http://www.pinterest.com/AmoebaSister­s Instagram: https://www.instagram.com/amoebasistersofficial/ Visit our Redbubble store at http://www.amoebasisters.com/store.html The Amoeba Sisters videos demystify science with humor and relevance. The videos center on Pinky's certification and experience in teaching science at the high school level. Pinky's teacher certification is in grades 4-8 science and 8-12 composite science (encompassing biology, chemistry, and physics). Amoeba Sisters videos only cover concepts that Pinky is certified to teach, and they focus on her specialty: secondary life science. For more information about The Amoeba Sisters, visit: http://www.amoebasisters.com/about-us.html We cover the basics in biology concepts at the secondary level. If you are looking to discover more about biology and go into depth beyond these basics, our recommended reference is the FREE, peer reviewed, open source OpenStax biology textbook: https://openstax.org/details/books/biology We take pride in our AWESOME community, and we welcome feedback and discussion. However, please remember that this is an education channel. See YouTube's community guidelines https://www.youtube.com/yt/policyandsafety/communityguidelines.html and YouTube's policy center https://support.google.com/youtube/topic/2676378?hl=en&ref_topic=6151248. We also reserve the right to remove comments with vulgar language. Music is this video is listed free to use/no attribution required from the YouTube audio library https://www.youtube.com/audiolibrary/music?feature=blog We have YouTube's community contributed subtitles feature on to allow translations for different languages. YouTube automatically credits the different language contributors below (unless the contributor had opted out of being credited). We are thankful for those that contribute different languages. If you have a concern about community contributed contributions, please contact us.
Views: 1069815 Amoeba Sisters
What are Enzymes, Substrate and Product? - BiochemDen.com
 
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Visit: https://www.biochemden.com/enzyme-basic-video-presentation/ Enzymes are macromolecular biological catalysts. Enzymes accelerate chemical reactions. The molecules upon which enzymes may act are called substrates and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called enzymology and a new field of pseudo-enzyme analysis has recently grown up, recognising that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudo catalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. The latter are called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction rate by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many therapeutic drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH. Follow: Blog: https://www.biochemden.com Facebook: https://www.facebook.com/BiochemDen Twitter: https://twitter.com/biochemden Google Plus: https://plus.google.com/+BiochemdenIn Pinterest: https://www.pinterest.com/biochemden/ Telegram: https://t.me/biochemden #BiochemDen #Biochemistry #Metabolism #BiochemistryResources #Biochem #Biomolecules #biochemistry #Biochemden #Biochemistryeducation
Views: 76 Biochemistry Den
3.6.3 Explain factors affecting enzyme activity
 
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Temperature: As temperature increases so to does the kinetic energy of the enzyme and substrate molecules which randomly collide. The frequency of collisions increases as the temperature increases thus initially increasing the rate of reaction. This occurs up to a maximum rate of reaction and the temperature at which the maximum rate of reaction is reached is referred to as the optimum temperature. Beyond the optimum temperature, increasing temperature increases the kinetic energy of the molecules to the point that the three-dimensional shape of the enzyme can be lost. Thus the shape of its active site changes and can no longer bind to the substrate, reducing the rate of reaction beyond the optimum temperature. pH: All enzymes have an optimum pH at which they have their maximum rate of reaction. Increasing pH values are as a result of the addition of hydroxide ions (OH-) while decreasing pH values are as a result of the addition of hydrogen ions (H+). The addition of either OH- or H+ can change the charges of the amino acids that make up the polypeptide chains of the enzyme. This can alter the bonding in the protein and change the shape of the active site resulting in denaturation, or alternatively it can prevent the substrate from binding with the enzyme's active site. Therefore either increasing or decreasing pH from the optimum value results in decreasing rate of enzyme activity. Substrate concentration: When discussing substrate concentration it is assumed that enzyme concentration remains constant. When substrate concentration is increased the rate of enzyme activity increases as the enzyme's active sites are gradually filled through the increased number of collisions with the substrate (due to increased substrate concentration). However, there comes a point when all of the enzyme's active sites are bound with substrates and the enzyme's are working at their maximum rate of reaction. Any increase in substrate concentration beyond this point will not result in any additional increase in rate of enzyme activity.
Views: 141455 Stephanie Castle
Enzyme Function and Inhibition
 
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This video animation describes the basics of enzyme structure and function. This includes enzyme substrates and active sites, enzyme denaturation, and competitive and non-competitive inhibition. This entire case study can be found on the National Center for Case Study Teaching in Science website at the following address: http://sciencecases.lib.buffalo.edu/cs/collection/detail.asp?case_id=819&id=819
Enzymatic Reactions: Types of Reactions & Enzymes – Biochemistry | Lecturio
 
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This video “Enzymatic Reactions: Types of Reactions & Enzymes” is part of the Lecturio course “Biochemistry” ► WATCH the complete course on http://lectur.io/emzymaticreactions ► LEARN ABOUT: - Types of Enzymatic reactions - Single substrate – Single product - Single substrate – Multiple products - Multiple substrates – Single products - Multiple substrates – Multiple products - How enzymes bind substrates - Their ability to catalyzed reactions - Chemical catalyst - How substrates affect enzymes on binding - The interaction of the enzymes - ES complex (Enzyme substrate complex) - Changes of shape of the enzyme - ES* complex - Transfer of one substrate to another - EP complex (Enzyme product complex) - The steps of catalysis ► THE PROF: Your lecturer is Professor Kevin Ahern. He is currently teaching biochemistry and biophysics at the Oregon State University, where he has also successfully completed his Ph.D. in biochemistry. Beside writing poetry and songs about several topics including medical ones—believe it or not as well—he has written the popular ebooks “Biochemistry Free and Easy” and "Kevin and Indira's Guide to Getting Into Medical School." His edutaining videos on YouTube were watched over 2.75 million times making him a medical education YouTube star. ► LECTURIO is your single-point resource for medical school: Study for your classes, USMLE Step 1, USMLE Step 2, MCAT or MBBS with video lectures by world-class professors, recall & USMLE-style questions and textbook articles. Create your free account now: http://lectur.io/emzymaticreactions ► INSTALL our free Lecturio app iTunes Store: https://app.adjust.com/z21zrf Play Store: https://app.adjust.com/b01fak ► READ TEXTBOOK ARTICLES related to this video: Enzymes – Biocatalysts of Metabolism http://lectur.io/enzymaticreactionsarticle ► SUBSCRIBE to our YouTube channel: http://lectur.io/subscribe ► WATCH MORE ON YOUTUBE: http://lectur.io/playlists ► LET’S CONNECT: • Facebook: https://www.facebook.com/lecturio.medical.education.videos • Instagram: https://www.instagram.com/lecturio_medical_videos • Twitter: https://twitter.com/LecturioMed
√ The effects of substrate concentration on enzymes | Biology
 
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#iitutor #Biology #Enzymes https://www.iitutor.com As mentioned in the experiment ‘The effects of pH on Enzymes’: This enzyme facilitates the decomposition of hydrogen peroxide (a toxic by-product of the body) into water and oxygen. The reaction of catalase in the decomposition of living tissue. We have already discovered the optimum pH level is pH7, this experiment looks at varying concentrations of the substrate, and its effect on the rate of activity. Hypothesis: When hydrogen peroxide is added in various concentrations, the enzyme reaction rate will increase with increasing substrate concentration. 1. Place catalase paper 30mL of Hydrogen peroxide 0.3% solution. 2. Using a stopwatch, determine how long it takes for reaction to take place. 3. Repeat steps 1-2 with catalase in solutions of 30mL of Hydrogen peroxide 0.7%, Hydrogen peroxide 1.5% and Hydrogen peroxide 3.0%. 4. Record results in a table and draw a graph of the results. Do your results support your hypothesis? How could you improve this experiment? Name any safety precautions you followed. Your results illustrate that with increasing substrate concentration, the reaction rate is faster. However beyond 1.5% of hydrogen peroxide, the enzyme is saturated (all active sites are taken) with substrate. This means at 3.0% hydrogen peroxide, the reaction does not increase, nor decrease, it plateaus. This means the reaction is working at its maximum rate, and will continue working at that rate until all substrates are broken down. The only way the reaction rate would increase, is if more enzyme was added to the solution. Therefore, the rate of reaction is in proportion to the substrate concentration.
Views: 5446 iitutor.com
Enzyme and Substrate -Lock and Key
 
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This is for education only! (It's my school hw) -- Created using PowToon -- Free sign up at http://www.powtoon.com/youtube/ -- Create animated videos and animated presentations for free. PowToon is a free tool that allows you to develop cool animated clips and animated presentations for your website, office meeting, sales pitch, nonprofit fundraiser, product launch, video resume, or anything else you could use an animated explainer video. PowToon's animation templates help you create animated presentations and animated explainer videos from scratch. Anyone can produce awesome animations quickly with PowToon, without the cost or hassle other professional animation services require.
Views: 6825 G connect
What is substrate and enzyme
 
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What is substrate and enzyme
Enzymes and activation energy | Biomolecules | MCAT | Khan Academy
 
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Explore the role of enzymes in making a reaction more likely to happen quickly. By Ross Firestone. Created by Ross Firestone. Watch the next lesson: https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-structure-and-function/v/the-induced-fit-model-of-enzyme-catalysis?utm_source=YT&utm_medium=Desc&utm_campaign=mcat Missed the previous lesson? https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-structure-and-function/v/an-introduction-to-enzymes-and-catalysis?utm_source=YT&utm_medium=Desc&utm_campaign=mcat MCAT on Khan Academy: Go ahead and practice some passage-based questions! About Khan Academy: Khan Academy offers practice exercises, instructional videos, and a personalized learning dashboard that empower learners to study at their own pace in and outside of the classroom. We tackle math, science, computer programming, history, art history, economics, and more. Our math missions guide learners from kindergarten to calculus using state-of-the-art, adaptive technology that identifies strengths and learning gaps. We've also partnered with institutions like NASA, The Museum of Modern Art, The California Academy of Sciences, and MIT to offer specialized content. For free. For everyone. Forever. #YouCanLearnAnything Subscribe to Khan Academy’s MCAT channel: https://www.youtube.com/channel/UCDkK5wqSuwDlJ3_nl3rgdiQ?sub_confirmation=1 Subscribe to Khan Academy: https://www.youtube.com/subscription_center?add_user=khanacademy
Views: 196673 khanacademymedicine
Enzyme Substrate Interaction | Lock and Key Concept of Enzyme
 
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Enzyme-substrate complex The intermediate formed when a substrate molecule interacts with the active site of an enzyme. Following the formation of an enzyme-substrate complex, the substrate molecule undergoes a chemical reaction and is converted into a new product. Various mechanisms for the formation of enzyme-substrate complexes have been suggested, including the induced-fit model and the lock-and-key mechanism. The enzyme-substrate complex is a temporary molecule formed when an enzyme comes into perfect contact with its substrate. Without its substrate, an enzyme is a slightly different shape. The substrate causes a conformational change, or shape change when the substrate enters the active site. The active site is the area of the enzyme capable of forming weak bonds with the substrate. This shape change can force two or more substrate molecules together, or split individual molecules into smaller parts. Most reactions that cells use to stay alive require the actions of enzymes to happen fast enough to be useful. These enzymes are directly coded for in the DNA of the organism. The enzyme substrate complex is extremely important for a number of reasons. First, the enzyme substrate complex is only temporary. This means that once the substrate has changed, it can no longer bind to the enzyme. The products are released and the enzyme is ready for another substrate molecule. A single enzyme can operate repeatedly millions of times, meaning only a small amount of enzyme is needed in each cell. (Credit- https://biologydictionary.net/enzyme-substrate-complex/) Solution-Pharmacy- The solution-Pharmacy is the completely dedicated channel for Pharmacy Profession. Here we provide Free MCQs, Flashcard and Most Importantly Practical Videos for all Students. Find us in all leading Social Network to Stay Connected- Website- https://pushpendrakpatel.wixsite.com/solution Facebook Page- www.facebook.com/pharmavideo/ Facebook Group- https://www.facebook.com/groups/solutionpharamcy E-Mail- [email protected] Instagram- https://www.instagram.com/solutionpharmacy/ LinkedIn- http://linkedin.com/in/pushpendrakpatel
Views: 164 Solution- Pharmacy
Feedback Inhibition: Substrate, Enzyme, and End Product
 
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#feedbackinhibition Hey! This video is about Feedback Inhibition. We will be studying about #substrates, #enzymes, and end products. Check it out and see how it all works! Was this video helpful? Feel free to subscribe, like, and comment! Get your FREE Micro Mini Course here 🔬 Microbiology Mini Course http://the-roc-a-strong-foundation.thinkific.com/courses/mini --------------------------------------------------------------------- Freshman Level 🔬 Microbiology Checklist http://eepurl.com/gaCagz 🔬 Microbiology E-Workbook http://the-roc-a-strong-foundation.thinkific.com/courses/book 🔬 Microbiology Mini Course http://the-roc-a-strong-foundation.thinkific.com/courses/mini Sophomore Level 🔬 5-Day Challenge to Better Studying {Spring 2019} 🔬 Done-For-You Microbiology Study Program http://the-roc-a-strong-foundation.thinkific.com/courses/dfy Junior Level 🔬 Microbiology Study Program http://the-roc-a-strong-foundation.thinkific.com/courses/consult Senior Level 🔬 How to Be Success in Microbiology Even If You Don’t Know What You’re Doing Webinar {Spring 2019} 🔬 Microbiology Study Program (Full Package) http://the-roc-a-strong-foundation.thinkific.com/courses/full ---------------------------------------------------------------------- Facebook www.facebook.com/TheROCastrongfoundation/ Instagram https://www.instagram.com/microbiologytutor/ Twitter https://twitter.com/ROCstrgfndation --------------------------------------------------------------------- Hey! I’m so glad you made it here! My name is Rochelle Harris. I’m your microbiology tutor. I take you outside the box of traditional studying and introduce you to an interactive and repetitive method of studying, so that you will remember the material. I’ve helped students through my teach, study with, and test your knowledge study method and I’m ready to take your studying up a notch. Over the past 3 years I have developed a 4-step microbiology study method that will not only save you time but allow you to absorb and retain the information during your study time. When I don’t have my head in microbiology, I love to head over to the Santa Monica beach or chill in Burbank at a park. I have to confess, my guilty pleasure is a good romance, suspense, and mystery novel. --------------------------------------------------------------------- What I listen to… Worship Playlist https://www.youtube.com/playlist?list=PLqGr3HGbS1ohzkV1_xVe1xiPbXWJTugbH --------------------------------------------------------------------- Business Inquiries [email protected]
Enzyme kinetics vmax and km
 
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Enzyme kinetics biochemistry vmax and Km lecture - This lecture explains about the enzyme kinetics of the enzyme reaction that includes explanation of vmax and Km. Maximum velocity of the enzyme substrate reaction and enzyme affinity towards a reaction is also explained with this video lecture. For more information, log on to- http://www.shomusbiology.com/ Get Shomu's Biology DVD set here- http://www.shomusbiology.com/dvd-store/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching the biochemistry lecture on enzyme kinetics reaction.
Views: 92364 Shomu's Biology
Feedback Inhibition of Biochemical Pathways [HD Animation]
 
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Feedback Inhibition of Biochemical Pathways Animation #Please → Like, comment, share and subscribe 👍🏻❤️
Substrates and Products in Chemical Reactions
 
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Synthetic Biology One is a free, open online course in synthetic biology beginning at the undergraduate level. We welcome scientists, artists, journalists, policymakers, or anyone interested in designing with DNA. Meet us at syntheticbiology1.com!
Induced fit model of enzyme catalysis | Chemical Processes | MCAT | Khan Academy
 
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Get a better appreciation for how enzymes and substrates bind together. By Ross Firestone. Created by Ross Firestone. Watch the next lesson: https://www.khanacademy.org/test-prep/mcat/chemical-processes/enzymes/v/the-six-types-of-enzymes?utm_source=YT&utm_medium=Desc&utm_campaign=mcat Missed the previous lesson? https://www.khanacademy.org/test-prep/mcat/chemical-processes/enzymes/v/an-introduction-to-enzymes-and-catalysis?utm_source=YT&utm_medium=Desc&utm_campaign=mcat MCAT on Khan Academy: Go ahead and practice some passage-based questions! About Khan Academy: Khan Academy offers practice exercises, instructional videos, and a personalized learning dashboard that empower learners to study at their own pace in and outside of the classroom. We tackle math, science, computer programming, history, art history, economics, and more. Our math missions guide learners from kindergarten to calculus using state-of-the-art, adaptive technology that identifies strengths and learning gaps. We've also partnered with institutions like NASA, The Museum of Modern Art, The California Academy of Sciences, and MIT to offer specialized content. For free. For everyone. Forever. #YouCanLearnAnything Subscribe to Khan Academy’s MCAT channel: https://www.youtube.com/channel/UCDkK5wqSuwDlJ3_nl3rgdiQ?sub_confirmation=1 Subscribe to Khan Academy: https://www.youtube.com/subscription_center?add_user=khanacademy
Views: 191316 khanacademymedicine
Enzyme inhibition
 
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For more information, log on to- http://shomusbiology.weebly.com/ Download the study materials here- http://shomusbiology.weebly.com/bio-materials.html An enzyme inhibitor is a molecule, which binds to enzymes and decreases their activity. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. They are also used as herbicides and pesticides. Not all molecules that bind to enzymes are inhibitors; enzyme activators bind to enzymes and increase their enzymatic activity, while enzyme substrates bind and are converted to products in the normal catalytic cycle of the enzyme. The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalyzing its reaction. Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically (e.g. via covalent bond formation). These inhibitors modify key amino acid residues needed for enzymatic activity. In contrast, reversible inhibitors bind non-covalently and different types of inhibition are produced depending on whether these inhibitors bind to the enzyme, the enzyme-substrate complex, or both. Many drug molecules are enzyme inhibitors, so their discovery and improvement is an active area of research in biochemistry and pharmacology. A medicinal enzyme inhibitor is often judged by its specificity (its lack of binding to other proteins) and its potency (its dissociation constant, which indicates the concentration needed to inhibit the enzyme). A high specificity and potency ensure that a drug will have few side effects and thus low toxicity. Enzyme inhibitors also occur naturally and are involved in the regulation of metabolism. For example, enzymes in a metabolic pathway can be inhibited by downstream products. This type of negative feedback slows the production line when products begin to build up and is an important way to maintain homeostasis in a cell. Other cellular enzyme inhibitors are proteins that specifically bind to and inhibit an enzyme target. This can help control enzymes that may be damaging to a cell, like proteases or nucleases. A well-characterised example of this is the ribonuclease inhibitor, which binds to ribonucleases in one of the tightest known protein--protein interactions.[1] Natural enzyme inhibitors can also be poisons and are used as defences against predators or as ways of killing prey. Source of the article published in description is Wikipedia. I am sharing their material. Copyright by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page PPT source- National Taiwan University, Jaung Web. Copywright by original content developer. Link- http://juang.bst.ntu.edu.tw/BCbasics/Animation.htm
Views: 39348 Shomu's Biology
Enzyme kinetics animation
 
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This animation explains about the enzyme kinetics vmax km. http://shomusbiology.com/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction is investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how it activity is controlled, and how a drug or an agonist might inhibit the enzyme. Enzymes are usually protein molecules that manipulate other molecules — the enzymes' substrates. These target molecules bind to an enzyme's active site and are transformed into products through a series of steps known as the enzymatic mechanism. These mechanisms can be divided into single-substrate and multiple-substrate mechanisms. Kinetic studies on enzymes that only bind one substrate, such as triosephosphate isomerase, aim to measure the affinity with which the enzyme binds this substrate and the turnover rate. Some other examples of enzymes are phosphofructokinase and hexokinase, both of which are important for cellular respiration (glycolysis). When enzymes bind multiple substrates, such as dihydrofolate reductase (shown right), enzyme kinetics can also show the sequence in which these substrates bind and the sequence in which products are released. An example of enzymes that bind a single substrate and release multiple products are proteases, which cleave one protein substrate into two polypeptide products. Others join two substrates together, such as DNA polymerase linking a nucleotide to DNA. Although these mechanisms are often a complex series of steps, there is typically one rate-determining step that determines the overall kinetics. This rate-determining step may be a chemical reaction or a conformational change of the enzyme or substrates, such as those involved in the release of product(s) from the enzyme. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page Animation source: Essential biochemistry, enzyme kinetics link- http://www.wiley.com/college/pratt/0471393878/instructor/animations/enzyme_kinetics/index.html
Views: 63557 Shomu's Biology
Derivation of Enzyme Kinetics for Competitive Inhibition
 
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Derives the rate expression for an enzyme reaction with a substrate to make a product where an inhibitor competes for the enzyme to form an inactive complex; this is competitive inhibition. The rate determining step approximation is used to determine the rate expression. Check out our screencasts on other types of inhibition: https://www.youtube.com/playlist?list=PL4xAk5aclnUj26ubv86C34HL703ZD_bsF Made by faculty at the University of Colorado Boulder, Department of Chemical & Biological Engineering. Check out our Kinetics/Reactor Design playlists: https://www.youtube.com/user/LearnChemE/playlists?view=50&flow=list&shelf_id=7 Check out our website for screencasts organized by popular textbooks: http://www.learncheme.com/screencasts/kinetics-reactor-design
Views: 14871 LearnChemE
√ How does Substrate Concentration affect Enzyme Activity | Biology
 
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#iitutor #Biology #SubstrateConcentration https://www.iitutor.com Factors that influence the enzyme that have the ability to alter or reduce their effectiveness include: Temperature, pH, Substrate concentration, Cofactors, Inhibitors (deactivate enzymes to purposely slow their activity temporarily or permanently). The concentration of substrate affects enzyme activity. The rate of an enzyme controlled reaction is affected by the concentration of the substrate. An increase in substrate concentration will increase the rate of reaction until all enzyme active sites are occupied. The higher the substrate concentration, the greater the rate of enzyme reaction, until all available enzyme active sites are being used to catalyse reactions. When all enzymes have a substrate each, the reaction rate plateaus. This is because the reaction rate is working at its maximum capacity. Increasing the substrate concentration beyond the saturation point will not increase the rate of reaction, since all enzymes are working at their maximum turnover rate and will have to be reused to act on the additional substrate. The only way to increase the reaction rate would be to increase the enzyme concentration.
Views: 13065 iitutor.com
Feedback Inhibition or End Product Inhibition of Enzymes
 
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This video explains Feed back inhibition or allosteric modulation of enzymes with animation. What are enzymes? What is an active site? How is it different from allosteric site?
Views: 37488 biologyexams4u
Enzyme catalysis
 
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For more information, log on to- http://shomusbiology.weebly.com/ Download the study materials here- http://shomusbiology.weebly.com/bio-materials.html Enzyme catalysis is the catalysis of chemical reactions by specialized proteins known as enzymes. Catalysis of biochemical reactions in the cell is vital due to the very low reaction rates of the uncatalysed reactions.[citation needed] The mechanism of enzyme catalysis is similar in principle to other types of chemical catalysis. By providing an alternative reaction route the enzyme reduces the energy required to reach the highest energy transition state of the reaction. The reduction of activation energy (Ea) increases the number of reactant molecules with enough energy to reach the activation energy and form the product. The favored model for the enzyme-substrate interaction is the induced fit model.[1] This model proposes that the initial interaction between enzyme and substrate is relatively weak, but that these weak interactions rapidly induce conformational changes in the enzyme that strengthen binding. The advantages of the induced fit mechanism arise due to the stabilizing effect of strong enzyme binding. There are two different mechanisms of substrate binding: uniform binding, which has strong substrate binding, and differential binding, which has strong transition state binding. The stabilizing effect of uniform binding increases both substrate and transition state binding affinity, while differential binding increases only transition state binding affinity. Both are used by enzymes and have been evolutionarily chosen to minimize the Ea of the reaction. Enzymes which are saturated, that is, have a high affinity substrate binding, require differential binding to reduce the Ea, whereas small substrate unbound enzymes may use either differential or uniform binding. These effects have led to most proteins using the differential binding mechanism to reduce the Ea, so most proteins have high affinity of the enzyme to the transition state. Differential binding is carried out by the induced fit mechanism - the substrate first binds weakly, then the enzyme changes conformation increasing the affinity to the transition state and stabilizing it, so reducing the activation energy to reach it. It is important to clarify, however, that the induced fit concept cannot be used to rationalize catalysis. That is, the chemical catalysis is defined as the reduction of Ea‡ (when the system is already in the ES‡) relative to Ea‡ in the uncatalyzed reaction in water (without the enzyme). The induced fit only suggests that the barrier is lower in the closed form of the enzyme but does not tell us what the reason for the barrier reduction is. Induced fit may be beneficial to the fidelity of molecular recognition in the presence of competition and noise via the conformational proofreading Source of the article published in description is Wikipedia. I am sharing their material. Copyright by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page PPT source- National Taiwan University, Jaung Web. Copywright by original content developer. Link- http://juang.bst.ntu.edu.tw/BCbasics/Animation.htm
Views: 23701 Shomu's Biology
Induced Fit Model of Enzyme Action
 
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The induced fit model refers to the interaction between the enzyme and the substrate. The substrate binds to the active site of the enzyme due to a complementary shape. Once the substrate has bound the enzyme changes shape slightly to form an even more exact fit (induced fit). The enzyme then catalyses the reaction and releases the product(s) so that the process can occur again. For more Biology video lessons check out www.anytimeeducation.com
Views: 12254 Jeremy LeCornu
Enzymes: Mr. W's Enzyme Song
 
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On iTunes at https://itunes.apple.com/us/artist/glenn-wolkenfeld/id555040717 On Amazon at http://tinyurl.com/pvt5kbb Take the enzymes interactive quiz: http://www.sciencemusicvideos.com/quizzes/ Buy the video at http://www.teacherspayteachers.com/Store/Glenn-Wolkenfeld-1 Get curriculum at http://www.sciencemusicvideos.com On twitter, https://twitter.com/GlennWolkenfeld for bio-haiku and verse. This movie explains the biology of enzymes. My hope is that it will catalyze lots of learning. Enzymes LYRICS: They're the protein catalysts in every organism ENZYMES! Through enzymatic action your metabolism's driven ENZYMES! In staphylococcus, jellyfish, tarantulas and trees, They lower activation energy Enzymes, in you and me now ENZYMES! You got 'em in your cells where they do cellular digestion, ENZYMES! You got 'em in your mouth and in your stomach and intestines ENZYMES! The thing an enzyme acts upon is called a substrate. They fit like lock and key with complementary shape Enzymes, speed up reaction rates ENZYMES! An enzyme binds its substrate at its active site ENZYMES! Bound together in a complex where they snuggle so tight, ENZYMES! New bonds will form and break due to the active site's chemistry Reactants become products, it's the enzyme's specialty, Product gets release enzyme repeats its action readily ENZYMES! Like any molecule an enzyme's shape defines its function. ENZYMES! Environmental change that changes shape leads to malfunction, ENZYMES! Every enzyme has a pH where it catalyzes best, a pH change will set enzyme activity to rest. Enzymes are so sensitive they're easily upset ENZYMES! More heat until a certain point increases their efficiency ENZYMES! But too much heat denatures them destroying their activity ENZYMES! That's why a fever running high's a dangerous situation, All that heat can alter enzymatic conformation. Keep it 98.6 for enzyme optimization ENZYMES! Enzymes in saliva will break starch into glucose ENZYMES! If you lack the enzyme lactase then you won't enjoy milk lactose, ENZYMES! Tay-sachs, galactosemia and PKU disease, All caused by inherited enzyme deficiencies ENZYMES, they're what everybody needs ENZYMES!
Views: 269632 sciencemusicvideos
Derivation of Enzyme Kinetics for Noncompetitive Inhibition
 
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Derives the rate expression for an enzyme reaction with a substrate to make a product where an inhibitor competes for the substrate and it also competes for the enzyme-substrate complex to form an inactive complex; this is noncompetitive inhibition (or mixed inhibition). The rate determining step approximation is used to determine the rate expression. Check out our screencasts on other types of inhibition: https://www.youtube.com/playlist?list=PL4xAk5aclnUj26ubv86C34HL703ZD_bsF Made by faculty at the University of Colorado Boulder, Department of Chemical & Biological Engineering. Check out our Kinetics/Reactor Design playlists: https://www.youtube.com/user/LearnChemE/playlists?view=50&flow=list&shelf_id=7 Check out our website for screencasts organized by popular textbooks: http://www.learncheme.com/screencasts/kinetics-reactor-design
Views: 11392 LearnChemE
Enzyme
 
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Enzymes enable molecules called substrates to undergo a chemical change to create new molecules called products. Each substrate fits in a specific area of the enzyme called the active site similar to lock and key mechanism.
Views: 277402 kosasihiskandarsjah
ENZYMES (Hindi/English) Agricultural Field Officer IBPS
 
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ENZYMES A protein with catalytic properties due to its power of specific activation Enzymes are proteins that increase the rate of reaction by lowering the energy of activation They catalyze nearly all the chemical reactions taking place in the cells of the body. Not altered or consumed during reaction. Reusable Chemical reactions need an initial input of energy = THE ACTIVATION ENERGY During this part of the reaction the molecules are said to be in a transition state. Making reactions go faster Increasing the temperature make molecules move faster Biological systems are very sensitive to temperature changes. Enzymes can increase the rate of reactions without increasing the temperature. They do this by lowering the activation energy. They create a new reaction pathway “a short cut” Cofactors An additional non-protein molecule that is needed by some enzymes to help the reaction Tightly bound cofactors are called prosthetic groups Cofactors that are bound and released easily are called coenzymes Many vitamins are coenzymes The substrate The substrate of an enzyme are the reactants that are activated by the enzyme Enzymes are specific to their substrates The specificity is determined by the active site APOENZYME and HOLOENZYME The enzyme without its non protein moiety is termed as apoenzyme and it is inactive. Holoenzyme is an active enzyme with its non protein component Important Terms to Understand Biochemical NatureAnd Activity of Enzymes Cofactor: A cofactor is a non-protein chemical compound that is bound (either tightly or loosely) to an enzyme and is required for catalysis. Types of Cofactors: Coenzymes. Prosthetic groups. Types of Cofactors Coenzyme:The non-protein component, loosely bound to apoenzyme by non-covalent bond. Examples : vitamins or compound derived from vitamins. Prosthetic group The non-protein component, tightly bound to the apoenzyme by covalent bonds is called a Prosthetic group. The Lock and Key Hypothesis Fit between the substrate and the active site of the enzyme is exact Like a key fits into a lock very precisely The key is analogous to the enzyme and the substrate analogous to the lock. Temporary structure called the enzyme-substrate complex formed Products have a different shape from the substrate Once formed, they are released from the active site Leaving it free to become attached to another substrate The Induced Fit Hypothesis Some proteins can change their shape (conformation) When a substrate combines with an enzyme, it induces a change in the enzyme’s conformation The active site is then moulded into a precise conformation Making the chemical environment suitable for the reaction The bonds of the substrate are stretched to make the reaction easier (lowers activation energy) The effect of pH Extreme pH levels will produce denaturation The structure of the enzyme is changed The active site is distorted and the substrate molecules will no longer fit in it At pH values slightly different from the enzyme’s optimum value, small changes in the charges of the enzyme and it’s substrate molecules will occur This change in ionisation will affect the binding of the substrate with the active site. The effect of temperature Q10 (the temperature coefficient) = the increase in reaction rate with a 10°C rise in temperature. For chemical reactions the Q10 = 2 to 3(the rate of the reaction doubles or triples with every 10°C rise in temperature) Enzyme-controlled reactions follow this rule as they are chemical reactions BUT at high temperatures proteins denature The optimum temperature for an enzyme controlled reaction will be a balance between the Q10 and denaturation. Inhibitors Inhibitors are chemicals that reduce the rate of enzymic reactions. The are usually specific and they work at low concentrations. They block the enzyme but they do not usually destroy it. Many drugs and poisons are inhibitors of enzymes in the nervous system. The effect of enzyme inhibition Irreversible inhibitors: Combine with the functional groups of the amino acids in the active site, irreversibly. Examples: nerve gases and pesticides, containing organophosphorus, combine with serine residues in the enzyme acetylcholine esterase. Applications of inhibitors Negative feedback: end point or end product inhibition Poisons snake bite, plant alkaloids and nerve gases. Medicine antibiotics, sulphonamides, sedatives and stimulants Thanks for Watching Subscribe for More videos like on fb: https://www.facebook.com/Advance-Agricultural-Classes-209935129434632/ join our fb group: https://www.facebook.com/groups/1600626926901456/ Visit our Website: https://advanceagriclasses.com/ Follow us on Instagrame: https://www.instagram.com/advanceagriclasses.official/
Labster Virtual Lab: Enzyme Kinetics Simulation
 
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Get your free trial here: https://www.labster.com/courses/LabsterX/ENK/2014/about ABOUT THE VIRTUAL LAB SIMULATION In the Enzyme Kinetics case, students learn how substrates are converted into products by catalysis. Additionally, students learn about the kinetics of enzyme involving the Michaelis-Menten equation and various rate constants. Content regarding DNA mutation and hyperactivity are also covered. In this lab, students run experiments using the enzyme Alcohol Dehydrogenase on a wild and mutant type to learn about Asian Glow syndrome. SUMMARIZED LEARNING OUTCOMES - Learn the experimental design of enzyme kinetics - Understand the Michaelis-Menten model of enzyme kinetics - Analyze spectrophotometer data and calculate Km and Vmax - Understand that kinetics of an enzyme can be modified by genetic mutations - Understand inhibition kinetics by using several types of inhibitors DETAILED LAB DESCRIPTION Using spectrophotometer to measure enzyme reaction Students access a fully equipped workbench where they prepare the Alcohol Dehydrogenase reaction and measure the product of Acetylaldehyde using a spectrophotometer. Students learn about the concept of spectrophotometer, how to prepare a master mix and how to calculate dilution. Students prepare a reaction in a 1 ml cuvette and measure the amount of product formed using the spectrophotometer. Supplementary 3D animation illustrates what happens on the molecular level when the substrate and co-factor enter the active site; dialog explains the situation as product is formed. Students are also prompted with quiz questions during the 3D animation to test their understanding on concepts. In the interactive animation, students identify the substrate by clicking on the different molecules. For every measurement, students receive a progress curve displaying amounts of product formed over time. At the end of the experiment, results are presented as an Excel spreadsheet. Students must analyze their outcome data and plot their own Michaelis-Menten graph to find the Km and Vmax for each enzyme. By comparing Km and Vmax values of the wild type vs. mutant Alcohol Dehydrogenase, students will be able to understand the Asian Glow syndrome. With the newly added module of enzyme inhibition, students are asked to perform different enzyme inhibition experiments using three different inhibitors. To begin, Students measure product formation using several inhibitor concentrations, extract the data, create their own Lineweaver-Burk plot and solve the Ki. We have recently upgraded the Enzyme Kinetics lab by implementing a mathematically based simulator. This provides students with a larger flexibility in conducting their experiments. Students can change parameters such as substrate concentrations, enzyme concentrations, temperature or pH and receive the corresponding results. In this semi-guided module, students may experiment with different parameters in order to find the optimal temperature and pH to reach the highest initial reaction rate. Upon completing the Enzyme Kinetics lab, students will be familiar with the kinetics of enzyme Alcohol Dehydrogenase, performing the experiment as well as analyzing the data outcome. By using a real life example of Alcohol Dehydrogenase and the Asian Glow syndrome, students will be able to understand about enzyme kinetics and relate it to their own daily life.
Views: 5349 Labster
10.  Kevin Ahern's Biochemistry - Enzymes II
 
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1. Contact me at [email protected] / Friend me on Facebook (kevin.g.ahern) 2. Download my free biochemistry book at http://biochem.science.oregonstate.edu/biochemistry-free-and-easy 3. Take my free iTunes U course at https://itunes.apple.com/us/course/biochemistry/id556410409 4. Check out my free book for pre-meds at http://biochem.science.oregonstate.edu/biochemistry-free-and-easy 5. Lecturio videos for medical students - https://www.lecturio.com/medical-courses/biochemistry.course 6. Course video channel at http://www.youtube.com/user/oharow/videos?view=1 7. Check out all of my free workshops at http://oregonstate.edu/dept/biochem/ahern/123.html 8. Check out my Metabolic Melodies at http://www.davincipress.com/ 9. My courses can be taken for credit (wherever you live) via OSU's ecampus. For details, see http://ecampus.oregonstate.edu/soc/ecatalog/ecourselist.htm?termcode=all&subject=BB 10. Course materials at http://oregonstate.edu/instruct/bb450 Highlights Enzymes II 1. Km is the substrate concentration that gives Vmax/2. Vmax varies, depending on the amount of enzyme that one uses, but Km is a constant for a given enzyme. 2. The higher the Km of an enzyme, the LOWER its affinity for its substrate and conversely, a low Km is consistent with a high affinity of enzyme for substrate. 3. If one lets a reaction go for a long time, it will reach equilibrium. At equilibrium, the relative concentration of products and reactants do not change. Initial velocities of reactions are therefore measured so as to avoid allow the product to accumulate and favor the reverse reaction. 4. Lineweaver-Burk plots are alternative plots of V vs S data obtained by taking the inverse of each and plotting it, thus making a 1/V vs 1/[S] plot. 5. On a Lineweaver-Burk plot, the Y intercept is 1/Vmax and the X intercept is -1/Km. 6. The catalytic actions of enzymes are related to their ability to be flexible. Fischer proposed a model of catalysis called the Lock and Key model, describing enzymes as inflexible and the substrate as like a key fitting into a lock. 7. Koshland's Induced Fit model says that not only does the enzyme change the substrate, but the substrate also changes the enzyme shape. This transient change of shape may bring together molecular groups that may not be close together in the enzyme prior to the change in enzyme shape. 8. Chemical changes brought about by catalysis facilitate a change in enzyme shape to allow for the release of products. When this happens, the enzyme returns to its original shape. 9. "Perfect" enzymes are enzymes that have evolved to the point where any additional mutation will reduce their ability to catalyze reactions. They are not common. Perfect enzymes have a very high ratio of Kcat/K. The only thing that inhibits their ability to function more efficiently is the rate of diffusion of substrate in water. 10. The active site of an enzyme is the place in the enzyme where a reaction is catalyzed. A substrate is a molecule bound by an enzyme and acted upon it. 11. Sequential Displacement has two subsets. a. Random binding - the order of binding multiple substrates is not rigidly set. b. Ordered binding - Simple ordered binding - one substrate binds first followed by another followed by release of product. 12. Another non-covalent enzyme mechanism involving multiple substrates is called Double Displacement (or Ping-Pong). In this method, the enzyme only binds one substrate at a time, but switches back and forth between different states. 13. Allosterism occurs when a small molecule interacts with a protein and affects its activity. 14. Enzymatic reactions can be inhibited by reversible and irreversible processes. Reversible processes involve binding of an inhibitor and its subsequent release. Irreversible processes involve covalent attachment of a molecule to an enzyme. a. Competitive Inhibition - Occurs when the inhibitor competes with the substrate for the binding site on an enzyme. The greater the concentration of inhibitor, the greater the inhibition. Competitive inhibition can be overcome by increasing amounts of substrate. The apparent Vmax of competitive inhibition does not vary from the Vmax of the same reaction when uninhibited. The apparent Km, however, does vary. b. Non-competitive inhibition - This type of reversible inhibition occurs when an inhibitor binds to an enzyme at a site unrelated to the substrate binding site. In this case, the inhibitor's binding to the enzyme is unrelated to the binding of the substrate and the inhibitor does not have to have a structure like that of the substrate. Thus, the inhibitor and substrate don't compete with each other. The inhibitor can inhibit the enzyme (during its binding) without interference from the substrate. Therefore, increasing substrate concentrations cannot eliminate the effect of the inhibitor. In this case, the Vmax is lowered, but the Km is unchanged.
Views: 11130 Kevin Ahern
Enzymatic Reaction Substrate Inhibition Michaelis Menton Kinetics Derivation
 
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Support our channel: https://u.muxy.io/tip/bai_gaming https://paypal.me/BAIZEGAMING View ALL our playlists: https://www.youtube.com/channel/UCtISIvF1WYe5CzbidXBmlgA/playlists?flow=grid&view=1 Want to support our channel? Become a Patron at https://www.patreon.com/BAIZEGAMING Check out our funny images on our Tumblr! https://bai-gaming.tumblr.com/ Follow us to get the funniest tweets! https://twitter.com/BAI_ZE_GAMING
Views: 74 BAI GAMING
NEET BIO - Cell: Nature of enzyme action
 
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This video describes about nature of enzyme action, each enzyme(E) has a substrate(S) binding site in its molecule so that a highly reactive enzyme substrate complex(ES) is produced. This complex dissociates into its product(P).
Views: 2304 XLClasses
Function of Enzymes - How Does Enzymes Work?
 
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If you are looking online to purchase essential enzymes for your body , please use my amazon affiliate link: https://www.amazon.com/gp/product/B000GFSVPU/ref=as_li_tl?ie=UTF8&tag=easexetoloswe-20&camp=1789&creative=9325&linkCode=as2&creativeASIN=B000GFSVPU&linkId=ab3bfa3c836ef9e9d62eb931267fbf1f Enzyme functions by binding to one or more of the reactants in a reaction. The reactants that bind to the enzyme are known as the substrates of the enzyme. You can purchase products having essential enzymes from health designs store.http://www.healthdesigns.com/referral-program
Views: 72532 AF Media Group
Enzymes and Catalysts
 
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This video will discuss the basics of chemical reactions and the functions of enzymes as a catalyst. Teachers: This PowerPoint can be purchased from my online store. The link below will provide the details. https://www.teacherspayteachers.com/Product/Enzymes-and-Catalysts-PowerPoint-free-student-handout-2677210 Key Words: Enzyme Catalyst Protein Amino acid Exothermic Exogonic Endothermic Endergonic Chemical reaction Organic Carbon Hydrolysis Dehydration synthesis Activation energy Active site Chemistry
Views: 87724 Beverly Biology
4  Enzymes
 
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For more information, log on to- http://shomusbiology.weebly.com/ Download the study materials here- http://shomusbiology.weebly.com/bio-materials.html Enzymes /ˈɛnzaɪmz/ are large biological molecules responsible for the thousands of chemical interconversions that sustain life.[1][2] They are highly selective catalysts, greatly accelerating both the rate and specificity of metabolic reactions, from the digestion of food to the synthesis of DNA. Most enzymes are proteins, although some catalytic RNA molecules have been identified. Enzymes adopt a specific three-dimensional structure, and may employ organic (e.g. biotin) and inorganic (e.g. magnesium ion) cofactors to assist in catalysis. In enzymatic reactions, the molecules at the beginning of the process, called substrates, are converted into different molecules, called products. Almost all chemical reactions in a biological cell need enzymes in order to occur at rates sufficient for life. Since enzymes are selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell. Like all catalysts, enzymes work by lowering the activation energy (Ea‡) for a reaction, thus dramatically increasing the rate of the reaction. As a result, products are formed faster and reactions reach their equilibrium state more rapidly. Most enzyme reaction rates are millions of times faster than those of comparable un-catalyzed reactions. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts in that they are highly specific for their substrates. Enzymes are known to catalyze about 4,000 biochemical reactions.[3] A few RNA molecules called ribozymes also catalyze reactions, with an important example being some parts of the ribosome.[4][5] Synthetic molecules called artificial enzymes also display enzyme-like catalysis.[6] Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, pressure, chemical environment (e.g., pH), and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins into smaller molecules, making the meat easier to chew). Source of the article published in description is Wikipedia. I am sharing their material. Copyright by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page
Views: 5096 Shomu's Biology
Products, Reactants, Energy, and Enzymes
 
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What is the difference between products and reactants? What is an enzyme-substrate complex and how do they make it possible for life to exist? We answer all these questions.
Views: 581 Erb Science
11.  Kevin Ahern's Biochemistry - Enzymes III
 
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1. Contact me at [email protected] / Friend me on Facebook (kevin.g.ahern) 2. Download my free biochemistry book at http://biochem.science.oregonstate.edu/biochemistry-free-and-easy 3. Take my free iTunes U course at https://itunes.apple.com/us/course/biochemistry/id556410409 4. Check out my free book for pre-meds at http://biochem.science.oregonstate.edu/biochemistry-free-and-easy 5. Lecturio videos for medical students - https://www.lecturio.com/medical-courses/biochemistry.course 6. Course video channel at http://www.youtube.com/user/oharow/videos?view=1 7. Check out all of my free workshops at http://oregonstate.edu/dept/biochem/ahern/123.html 8. Check out my Metabolic Melodies at http://www.davincipress.com/ 9. My courses can be taken for credit (wherever you live) via OSU's ecampus. For details, see http://ecampus.oregonstate.edu/soc/ecatalog/ecourselist.htm?termcode=all&subject=BB 10. Course materials at http://oregonstate.edu/instruct/bb450 Highlights of Enzymes III Lecture 1.Chemicals, such as DIPF and iodoacetate, covalently (and irreversibly) bind to the side chains of specific amino acids (serine and cysteine, respectively) and if these side chains are essential for the catalytic action of the enzyme, the enzyme will not catalyze reactions after being treated with these chemicals. 2. Penicillin is a substance that resembles the substrate of an enzyme in bacteria that helps make the bacterial cell wall. When it binds to the enzyme, it inactivates the enzyme by covalently bonding to the active site, thus destroying the enzyme (and killing the bacterium containing it). An inhibitor of this type is known as a suicide inhibitor. Highlights Catalytic Mechanisms 1. Proteases catalyze the hydrolysis of peptide bonds in polypeptides. They are usually fairly specific for certain amino acids and cut at or near those amino acids. 2. Chymotrypsin is a protease whose activity has been closely studied. Conveniently, the activity of chymotrypsin can be studied using an artificial substrate which, when cleaved by the enzyme, releases a yellow product. 3. When the release of the colored substrate by the enzyme is studied, it appears to occur in two different rates. First there is a VERY rapid release of the colored substrate. After that initial burst of activity, the remaining yellow color is released slowly. 4. The reason appears to be that the reaction catalyzed occurs in two steps. The first step cleaves the bond to produce the yellow product, which is rapidly released. The other product of this reaction is the remainder of the substrate that is covalently linked to the enzyme. In order for the enzyme to bind another substrate molecule and release more yellow color, it must first release the covalently bound molecule. This step occurs slowly and explains why subsequent yellow molecules are released slowly - after the initial one is released, the enzyme must remove the covalently bound molecule, bind a new substrate, and cut the substrate and the continue the process repeatedly. 5. Chymotrypsin is an example of a protease that employs reactive serine in its active site. Such an enzyme is called a serine protease. Treatment of chymotrypsin with DIPF, which covalently links to serines, inactivates the enzyme. 6. Serine proteases form covalent intermediates with their polypeptide substrates. The first step involves nucleophilic attack of an alkoxide ion on the polypeptide substrate to form an acyl-enzyme intermediate. Formation of this intermediate results in cleavage of the peptide bond and release of the first polypeptide fragment. The acyl-enzyme intermediate is resolved by addition of water to release the other portion of the original polypeptide along with regeneration of the original enzyme active site. This last step occurs relatively slowly. 7. In the active site of chymotrypsin (and other serine proteases) is a so-called catalytic triad of amino acids that includes a serine hydrogen bonded to a histidine. The histidine is, in turn, hydrogen bonded to an aspartic acid residue in the active site. Each of the hydrogen bonds of the catalytic triad is important in the catalytic mechanism. The nucleophilic alkoxide ion on serine is made possible ultimately by interactions in the catalytic triad and these hydrogen bonds.
Views: 8389 Kevin Ahern
Enzyme Animation
 
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Enzyme- A substance produced by a living organism that acts as a catalyst to bring about a specific bio-chemical reaction. Substrate- Molecules that are acted upon by Enzymes. Product- The molecules created after an enzyme acts upon a substrate making it into a product. Competitive Inhibitor- A molecule that stops a substrate from being able to react with an enzyme and stopping products from being produced, it bonds to the active site to do so. Non-Competitive Inhibitor- A molecule that stops a substrate from being able to react with an enzyme by re-constructs the active site and stops products from being created, it does not bond to the active site but does bond to the enzyme. First the substrate approaches the enzyme and bonds causing it to be changed into products, however if an inhibitor is added it can stop that reaction from occurring by a competitive inhibitor taking the place in the active site not allowing the substrate to bond or by a non-competitive inhibitor bonding to the enzyme but not by the active site and re-constructing the active site making the substrate unable to bond.
Views: 1247 kayleygee216
Substrate,Reagent and product - JEE||NEET||CBSE (IITian Faculty)(Hindi)
 
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"IITian Faculty" explains the above concept in entertaining and conceptual manner.
enzyme substrate complex
 
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my mum confiscated my enzymes so i built this video out of anger.
Views: 78 BramDoesGaming
Michaelis-Menten Kinetics: Considerations & Time Relation – Biochemistry | Lecturio
 
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This video “Michaelis-Menten Kinetics: Considerations & Time Relation” is part of the Lecturio course “Biochemistry” ► WATCH the complete course on http://lectur.io/michaelismenten ► LEARN ABOUT: - Michaelis-Menten Graph - Concentration of product (P) in proportion to time - Concentration of enzyme substrate (ES) in proportion to time - Concentration of enzyme (E) in proportion to time - Concentration of substrate (S) in proportion to time - Pre-steady state conditions - Steady state conditions - Conversion of enzymes substrate complex into product ► THE PROF: Your lecturer is Professor Kevin Ahern. He is currently teaching biochemistry and biophysics at the Oregon State University, where he has also successfully completed his Ph.D. in biochemistry. Beside writing poetry and songs about several topics including medical ones—believe it or not as well—he has written the popular ebooks “Biochemistry Free and Easy” and "Kevin and Indira's Guide to Getting Into Medical School." His edutaining videos on YouTube were watched over 2.75 million times making him a medical education YouTube star. ► LECTURIO is your single-point resource for medical school: Study for your classes, USMLE Step 1, USMLE Step 2, MCAT or MBBS with video lectures by world-class professors, recall & USMLE-style questions and textbook articles. Create your free account now: http://lectur.io/michaelismenten ► INSTALL our free Lecturio app iTunes Store: https://app.adjust.com/z21zrf Play Store: https://app.adjust.com/b01fak ► READ TEXTBOOK ARTICLES related to this video: Enzymes – Biocatalysts of Metabolism http://lectur.io/michaelismentenarticle ► SUBSCRIBE to our YouTube channel: http://lectur.io/subscribe ► WATCH MORE ON YOUTUBE: http://lectur.io/playlists ► LET’S CONNECT: • Facebook: https://www.facebook.com/lecturio.medical.education.videos • Instagram: https://www.instagram.com/lecturio_medical_videos • Twitter: https://twitter.com/LecturioMed
Enzymes II
 
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This course is part of a series taught by Kevin Ahern at Oregon State University on General Biochemistry. For more information about online courses go to http://ecampus.oregonstate.edu/ http://www.youtube.com/playlist?list=PL850269AA28EF394A Also check out the free textbook "Biochemistry Free and Easy" at: http://biochem.science.oregonstate.edu 1. The Gibbs free energy is the energy available to do useful work in reactions. The change in the Gibbs free energy for a reaction is important because it determines whether a reaction is favored, unfavored, or at equilibrium. 2. Thus, when the Gibbs free energy change is negative, the reaction in question goes forward as written, but when the Gibbs free energy change is positive, the reaction goes in reverse. 3. A related term to G is G°', which is the Standard Gibbs Free Energy change. This refers to the Gibbs Free Energy change for a reaction under standard conditions. Since most reactions occur at non-standard conditions, G is much more useful than G°'. In fact, the sign of G°' does NOT tell the direction of a reaction, except under standard conditions. 4. Chemical reactions require activation energy (I'll call it G+ here) in order to get started. Catalysts (both enzymes and non-biological catalysts) act by lowering G+. Catalysts DO NOT CHANGE G. All they do is lower the energy required to activate the reaction. While enzymes speed reactions immensely, they therefore DO NOT CHANGE THE OVERALL REACTION CONCENTRATION AT EQUILIBRIUM. They simply allow the reaction to get to equilibrium faster. 5. G is affected by the concentration of reactants and products of a reaction by the following equation G = G°' + RTln[Products/Reactants] Thus, as product concentrations increase, the G will become more positive. 6. If one performs an experiment in which a fixed amount of enzyme is added to 20 different tubes, each containing a different amount of substrate (molecule that the enzyme catalyzes the reaction on) and then lets the reaction in each tube go for a fixed amount of time, one will create varying amounts of product when the tubes are analyzed. The greatest amount of product will be found in the tube which had the greatest amount of substrate. If one measures the concentrations of each product and divides by the time the reaction occurred, one obtains a velocity for each reaction. A plot of the velocity versus the substrate concentration (V versus S) from the experiment looks like the binding curve of myoglobin for oxygen - hyperbolic. 7. Velocity of an enzymatic reaction is measured as the concentration of product formed per time. 8. If one lets a reaction go for a long time, it will reach equilibrium. At equilibrium, the relative concentration of products and reactants do not change. Initial velocities of reactions are therefore measured so as to avoid allow the product to accumulate and favor the reverse reaction. 9. The catalytic action of enzymes appears to be related to their ability to be at least slightly flexible. Originally, Fischer proposed a model of catalysis called the Lock and Key model. It described enzymes as inflexible and the substrate as like a key fitting into a lock. While substrates do, in fact, fit into enzymes somewhat like a key, the enzyme is NOT inflexible. 10. Koshland's model of enzyme action, called the Induced Fit model says that not only does the enzyme change the substrate (via catalysis), but the substrate also changes the enzyme shape upon binding. This transient change of enzyme shape is important for catalysis because it may bring together molecular groups (such as a phosphate and a sugar) that may not be close together in the enzyme prior to the change in enzyme shape. Remember that enzymes also work by orienting substrates together in the proper way to maximize their likelihood of bouncing together in a way that leads to making a bond. 11. Chemical changes brought about by catalysis facilitate a last change in enzyme shape to allow for the release of the products. When this happens, the enzyme returns to its original shape and remains unchanged by acting to catalyze the reaction. 12. At very high concentrations of substrate, the enzyme gets overwhelmed (saturated) and a maximum velocity (Vmax) is approached. If one adds more enzyme, a higher maximum velocity will be reached. Vmax thus doesn't tell very much about an enzyme because its value depends on the amount of enzyme we use. 13. Km is the substrate concentration that gives an enzyme half its Vmax. Note that Km is a CONCENTRATION. 14. We define Km as the substrate concentration that gives Vmax/2. Whereas the Vmax varies, depending on the amount of enzyme that one uses, the Km is a constant for a given enzyme for its substrate.
Catabolic Enzyme and Substrate Reactant
 
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with Oreos
Views: 134 larzthellama
Enzymes 3.1
 
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Table of Contents: 00:00 - 3.1 Enzymes 00:04 - 3.1 Mode of action of enzymes 00:22 - 3.1 Mode of action of enzymes 00:25 - Enzyme structure 01:15 - 3.1 Mode of action of enzymes 01:17 - Enzymes 01:34 - 3.1 Mode of action of enzymes 01:36 - Enzymes- Active site 01:58 - Enzymes- active site and substrate 02:22 - The enzyme- substrate complex. 02:43 - The enzyme- substrate complex. 03:41 - Enzyme-product complex 04:14 - The Lock and Key Hypothesis 04:50 - Enzymes 05:09 - Enzymes-the induced fit hypothesis 05:47 - Enzymes-the induced fit hypothesis 05:56 - Enzymes 06:18 - Enzymes 06:33 - Enzymes and Chemical reactions 06:49 - 07:03 - Making reactions go faster 07:30 - 07:51 - Reaction pathway 07:52 - An enzyme controlled pathway 07:52 - Reaction pathway 07:53 - 07:53 - Making reactions go faster 07:54 - 08:25 - Reaction pathway 08:51 - An enzyme controlled pathway 09:07 - Catalase catalyzing the break down of H2O2 09:37 - Initial Rate of reaction
Views: 25 HYSA Classroom
Derivation of Enzyme Kinetics for Uncompetitive Inhibition
 
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Derives the rate expression for an enzyme reaction with a substrate to make a product where an inhibitor competes for the enzyme-substrate complex to form an inactive complex; this is uncompetitive inhibition. The rate determining step approximation is used to determine the rate expression. Check out our screencasts on other types of inhibition: https://www.youtube.com/playlist?list=PL4xAk5aclnUj26ubv86C34HL703ZD_bsF Made by faculty at the University of Colorado Boulder, Department of Chemical & Biological Engineering. Check out our Kinetics/Reactor Design playlists: https://www.youtube.com/user/LearnChemE/playlists?view=50&flow=list&shelf_id=7 Check out our website for screencasts organized by popular textbooks: http://www.learncheme.com/screencasts/kinetics-reactor-design
Views: 7975 LearnChemE