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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: 74179 Shomu's Biology
Substrate kinetics of Enzyme (Determination of Km and VMAX)
 
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Project Title: Development of e-contents on foundation course on analytical biochemistry and separation techniques Project Investigator: Dr. Charmy Kothari Module: Substrate kinetics of enzyme (determination of Km and VMAX)
Views: 2571 Vidya-mitra
B7 Determine Vmax and Michaelis constant (Km) by graphical means and explain [HL IB Chemistry]
 
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You need to know the 3 parts of the graph: a) initially linear since many free enzymes available at the lower concentration of substrate. b) rate begins to slow as substrate cannot always find a free enzyme (some are being used by other substrate) c) Saturated -- the enzymes are always in use -- increasing substrate will no longer increase rate. Adding inhibitors will change these graphs -- but this is for another assessment statement.
Views: 99325 Richard Thornley
Enzymes (Part 2 of 5) - Enzyme Kinetics and The Michaelis Menten Model
 
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Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam For Related Practice Problems with Worked Video Solutions on Enzymes, visit courses.moofuniversity.com. In this video, I discuss the Michaelis-Menton Model for Enzyme Kinetics. For a non-allosteric enzyme, reaction velocity plotted vs substrate concentration results in a hyperbolic graph. As substrate concentration increases, reaction velocity increases, at least until a certain point, where beyond a certain concentration, the reaction velocity remains the same; this the reaction’s maximum velocity or Vmax. At lower substrate concentrations, first order kinetics are observed, but at higher substrate concentrations, because of the Vmax plateau, 0th order kinetics are observed, due to the enzyme being saturated. The hyperbolic graph has a hyperbolic equation associated with it, relating reaction velocity to Vmax, substrate concentration [S], and Km (the Michaelis-Menton constant). The Km is a combination of rate constants from the steady state equation (shown in the video), and it is effectively a measure of affinity between the enzyme and its substrate. A higher Km indicates a lower affinity, while a lower Km indicates a higher affinity. Km is NOT Vmax/2. Km happens to be equal to the substrate concentration when the reaction running at Vmax/2. For a suggested viewing order of the videos, information on tutoring, personalized video solutions, and an opportunity to support Moof University financially, visit MoofUniversity.com, and follow Moof University on the different social media platforms. Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity SUPPORT MOOF UNIVERSITY: http://www.moofuniversity.com/support-moof/ BUY A T-SHIRT https://shop.spreadshirt.com/moofuniversity/ INFORMATION ABOUT TUTORING AND PERSONALIZED VIDEO SOLUTIONS: http://www.moofuniversity.com/tutoring/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity
Views: 204487 Moof University
Enzyme Kinetics Part 2- How to Calculate Km and Vmax
 
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In this video I have explained how to calculate the value of Km and Vmax for an enzyme substarte reaction using Michaelis-Menten equation. Thanks to Amanda Moulton for painstakingly recording this video.
Views: 8951 Dr.Mungli
An introduction to enzyme kinetics | Chemical Processes | MCAT | Khan Academy
 
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Created by Ross Firestone. Watch the next lesson: https://www.khanacademy.org/test-prep/mcat/chemical-processes/enzymes/v/allosteric-regulation-and-feedback-loops?utm_source=YT&utm_medium=Desc&utm_campaign=mcat Missed the previous 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 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: 307754 khanacademymedicine
Enzymes (Part 3 of 5) - Lineweaver Burk Plot - Double Reciprocal Plot
 
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Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam For Related Practice Problems with Worked Video Solutions on Enzymes, visit courses.moofuniversity.com. In this video, I discuss how the Lineweaver-Burk (or Double-Reciprocal) Plot works in association with hyperbolic equation and Michaelis-Menton kinetics. Hyperbolas, when it comes to math, are not simple to work with, which is why the hyperbolic equation relating to Michaelis-Menton kinetics is altered to give the Lineweaver Burk equation / Double Reciprocal plot. It basically turns the hyperbolic equation into a linear equation, which is much easier to work with. The graph becomes 1/V plotted versus 1/substrate concentration. The x intercept is equal to -1/Km, and the y intercept is equal to 1/Vmax, which makes it easy to calculate for either when the values for the intercepts are available. The slope of the line is equal to Km/Vmax. For a suggested viewing order of the videos, information on tutoring, personalized video solutions, and an opportunity to support Moof University financially, visit MoofUniversity.com, and follow Moof University on the different social media platforms. Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity SUPPORT MOOF UNIVERSITY: http://www.moofuniversity.com/support-moof/ BUY A T-SHIRT https://shop.spreadshirt.com/moofuniversity/ INFORMATION ABOUT TUTORING AND PERSONALIZED VIDEO SOLUTIONS: http://www.moofuniversity.com/tutoring/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity
Views: 124668 Moof University
Enzyme Kinetics (Km and Vmax) - Part 1
 
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The enzyme kinetics specially explaining their Km and Vmax is done in three parts. This is part 1, kindly watch other 3 parts to complete this series. Thanks to Amanda Moulton for painstakingly recording this video
Views: 39228 Dr.Mungli
Catalytic Efficiency of Enzymes (kcat/Km)
 
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Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/catalytic-efficiency-of-enzymes-kcat-km Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
Views: 72556 AK LECTURES
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: 60721 Shomu's Biology
Enzymes (Part 5 of 5) - Lineweaver Burk Plot Example
 
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Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam For Related Practice Problems with Worked Video Solutions on Enzymes, visit courses.moofuniversity.com. In this video, I basically do an example problem relating to Michaelis-Menton Kinetics, the Hyperbolic Equation, and the Lineweaver-Burk (Double Reciprocal) Plot. For a suggested viewing order of the videos, information on tutoring, personalized video solutions, and an opportunity to support Moof University financially, visit MoofUniversity.com, and follow Moof University on the different social media platforms. Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity SUPPORT MOOF UNIVERSITY: http://www.moofuniversity.com/support-moof/ BUY A T-SHIRT https://shop.spreadshirt.com/moofuniversity/ INFORMATION ABOUT TUTORING AND PERSONALIZED VIDEO SOLUTIONS: http://www.moofuniversity.com/tutoring/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity
Views: 81004 Moof University
Catalytic efficiency (kcat/km) and turn over number of enzyme
 
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This lecture explains about the catalytic efficiency and turnover number of enzyme and it also explains how to calculate enzyme catalytic efficiency and turnover number. Catalytic efficiency calculation is really important to understand how an enzyme functions along with the turnover number that says many information about the efficiency of the enzyme and the affinity of the enzyme in binding substrate. 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 Know more about catalytic efficiency and turnover number of enzyme in Shomu's Biology website. 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 biochemistry lecture on catalytic efficiency and turnover number of enzyme reactions.
Views: 17687 Shomu's Biology
Calculating enzyme efficiency
 
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In this video I work a problem that asks us to determine which enzyme is more efficient. I also explain the conditions in which it is useful to determine the Kcat by using the equation Kcat= Vmax/Km
Views: 7189 FortuneFavorsPrep
Quick Guide to Calculating Enzyme Activity
 
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Using Excel to do the Lineweaver-Burk plot
Views: 37891 Mark Temple
Enzymatic inhibition and Lineweaver Burke plots | Biomolecules | MCAT | Khan Academy
 
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Created by Ross Firestone. Watch the next lesson: https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-kinetics/v/cooperativity?utm_source=YT&utm_medium=Desc&utm_campaign=mcat Missed the previous lesson? https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-kinetics/v/steady-states-and-the-michaelis-menten-equation?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: 410803 khanacademymedicine
How to Calculate Km and Vmax using Lineweaver Burk Plot
 
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In this video I have explained how to calculate Km and Vmax of an enzyme in Lineweaver Burk double reciprocal plot. The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents −1/Km. It also gives a quick, visual impression of the different forms of enzyme inhibition. You Can Subscribe to my Channel for REGULAR UPDATES by clicking on SUBSCRIBE button above! You can follow me on my BLOG by clicking the link below http://drmungli.blogspot.com/ You can follow my Facebook page Biochemistry Made Easy by Dr Prakash Mungli, MD by clicking the link below. Here I post USMLE step-1 style MCQs and you can participate in discussion. https://www.facebook.com/drmungli
Views: 23694 Dr.Mungli
045-Kinetic Constants: Km & Vmax
 
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Discussion of the meaning and graphical determination of the kinetic constants of Km & Vmax
Steady states and the Michaelis Menten equation | Biomolecules | MCAT | Khan Academy
 
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Created by Ross Firestone. Watch the next lesson: https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-kinetics/v/enzymatic-inhibition-and-lineweaver-burke-plots?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/enzymes-and-their-local-environment?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: 482722 khanacademymedicine
Specific activity and turnover number of an enzyme
 
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Specific activity and turnover number of an enzyme
Views: 10333 Peter Klappa
Enzyme kinetics calculating VMAX and KM
 
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Project Name: e-Content for undergraduate students of science in graduate programmes Project Investigator: Dr. Mandira Sikdar Module Name: Enzyme kinetics calculating VMAX and KM
Views: 1315 Vidya-mitra
Km & Kcat | Biochemistry Tutorial
 
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Example of Km and Kcat from Educator.com’s Biochemistry class. Want more video tutorials? Our full lesson includes in-depth explanations and even more worked out examples. ►See the entire syllabus at https://www.educator.com/chemistry/biochemistry/hovasapian/?utm_source=YT&utm_medium=SEO&utm_campaign=BIOCHEMYT In this video, we’ll discuss km and kcat. You'll learn about the michaelis-Menten equation, second order rate constant, and enzyme's affinity. Like other instructors such as Khan Academy, Kevin Ahern, Moof University, and Armando Hasudungan? Our Biochemistry instructor is pretty awesome too. Professor Hovasapian carefully goes through how Proteins, Carbohydrates, Nucleic Acids and other biomolecules make life on Earth possible. Combining his triple degrees in Mathematics, Chemistry, and Classics, along with 10+ years of teaching experience, Professor Hovasapian expertly helps students understand difficult biochemical concepts. Raffi also teaches AP Chemistry, Multivariable Calculus, and Linear Algebra on Educator. So what are you waiting for? Join over 100K satisfied high school and college students who have aced their classes and exams with http://www.Educator.com’s videos.
Views: 20019 Educator.com
Calculate the rate of enzyme activity
 
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A presentation that will show you how to calculate the rate of a reaction from experimental data.
Views: 14560 Paul Scott
Enzyme inhibition
 
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In this video I discuss the various types of enzyme inhibition, and their graphs.
Views: 90335 FortuneFavorsPrep
enzyme kinetics Calculating Vmax and Km
 
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In this video I do a problem where we determine the Vmax and Km for a normal uninhibited enzyme, and then determine the same the values when it's inhibited. The values are then plotted on a graph, and the type of inhibition is determined from the graph.
Views: 48128 FortuneFavorsPrep
Why Km does not change with the enzyme concentration
 
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Why Km does not change with the enzyme concentration.
Views: 5624 Peter Klappa
How to calculate Vmax and Km from a Lineweaver and Burk plot
 
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A quick guide for my students on how to use excel to get Km and Vmax
Views: 134498 DrDavidSmith
Enzymes - Michaelis Menten Model - A Few More Details
 
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Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam For Related Practice Problems with Worked Video Solutions on Enzymes, visit courses.moofuniversity.com. In this video, I provide a few more details about Vmax and Km under certain situations. When substrate concentration = Km in the hyperbolic equation, V = Vmax/2 This explains the association of Km with Vmax/2. Km is equal to the substrate concentration when the reaction is at half its maximum velocity. When substrate concentration is much greater than Km in the hyperbolic equation, V = Vmax This basically says that at very high concentrations, the reaction will be running at maximum velocity. When substrate concentration is much less than Km (substrate concentration is effectively 0) in the hyperbolic equation, V is proportional to substrate concentration This basically says that at very small substrate concentrations, the reaction follows first order kinetics. For a suggested viewing order of the videos, information on tutoring, personalized video solutions, and an opportunity to support Moof University financially, visit MoofUniversity.com, and follow Moof University on the different social media platforms. Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity SUPPORT MOOF UNIVERSITY: http://www.moofuniversity.com/support-moof/ BUY A T-SHIRT https://shop.spreadshirt.com/moofuniversity/ INFORMATION ABOUT TUTORING AND PERSONALIZED VIDEO SOLUTIONS: http://www.moofuniversity.com/tutoring/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity
Views: 18676 Moof University
Biochemistry 9.3: Enzyme kinetics part 2
 
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A number of important catalytic constants for enzyme reactions: Km, v max, kcat and kcat/vmax. Each convey different information about an enzyme's activity!
Views: 20391 biochemistry rocks
B.7 Vmax and Km (HL)
 
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Applications and skills: Determination of the maximum rate of reaction (Vmax) and the value of the Michaelis constant (Km) for an enzyme by graphical means, and explanation of its significance.
Views: 10737 Mike Sugiyama Jones
Lineweaver Burk plot data analysis
 
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using a Lineweaver Burk plot to analyse enzyme data This work is licenced under the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ or send a letter to Creative Commons, 171 Second Street, Suite 300, San Francisco, California 94105, USA.
Views: 112917 Peter Klappa
Biochemistry 9.2: Enzyme kinetics part 1
 
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Kinetics of chemical reactions with and without enzyme; variation of the initial rate with substrate concentration. Introduction of the Michaelis Menten equation.
Views: 30978 biochemistry rocks
Physiological Significance of Michaelis Constant
 
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Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/michaelis-constant Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
Views: 41191 AK LECTURES
Determine the dissociation constant
 
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Determining the dissociation constant Ki for a competitive inhibitor
Views: 5536 Peter Klappa
Catalytic Efficiency of Enzymes (kcat/Km) - Part II
 
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Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/catalytic-efficiency-of-enzymes-kcat-km-part-ii Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
Views: 28222 AK LECTURES
Enzyme Kinetics (Km and Vmax) -Part 3
 
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Thanks to Amanda Moulton for painstakingly recording this video!
Views: 10807 Dr.Mungli
Enzyme Inhibition (Part 1 of 3) - Competitive Inhibitors
 
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Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam Questions Answered in This Video: - What are competitive inhibitors, and what is mechanism by which they act? - How do competitive inhibitors affect the values of KM and VMAX? - How do competitively inhibited reactions look on the hyperbolic graph and Lineweaver-Burk plot? Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity INFORMATION ABOUT TUTORING: http://www.moofuniversity.com/tutoring/ TO SUPPORT MOOF UNIVERSITY WITH A FINANCIAL CONTRIBUTION: http://www.moofuniversity.com/support-moof/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity Video Content Summary: Competitive inhibitors "compete" with substrate for binding the enzyme's active site. Free enzyme will bind either the substrate OR the competitive inhibitor. It cannot bind both at the same time. If the enzyme binds the substrate, the enzyme-substrate complex forms, and the enzyme can convert the substrate into product. If, however, a competitive inhibitor binds the active site, the enzyme-competitive inhibitor complex forms, which cannot proceed towards products, for the simple reason that the competitive inhibitor impedes the ability of the substrate to bind to the enzyme. Since a competitive inhibitor blocks the substrate from binding, the competitive inhibitor essentially lowers the affinity of enzyme for the substrate. Thus increasing the KM. Despite this, VMAX can still be reached with a high enough substrate concentration. If the substrate concentration is sufficiently high, the substrates will out-compete the competitive inhibitor for binding at the active site, thus effectively overcoming the effects of the inhibitor. The effects of a competitive inhibitor on an enzyme-catalyzed reaction are depicted in a variety of ways in the video, and it is shown what happens to the hyperbolic graph and the Lineweaver-Burk plot, otherwise known as the double reciprocal plot.
Views: 12718 Moof University
The meaning of Vmax and other enzyme parameters
 
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Looking at Vmax, Vmax/Km and Km This work is licenced under the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ or send a letter to Creative Commons, 171 Second Street, Suite 300, San Francisco, California 94105, USA.
Views: 34169 Peter Klappa
Interpretation of Michaelis-Menten Equation
 
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Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/michaelis-menten-equation Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
Views: 113487 AK LECTURES
Biochemistry I Calculating apparent Km Problem
 
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Made with Explain Everything
Views: 2090 Gowtham Ganesan
Enzyme question using MM equation
 
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Enzyme questions part 1 http://biochemjm.wordpress.com/2014/03/07/enzymes-part-1-questions/ Enzyme questions part 2 http://biochemjm.wordpress.com/2014/03/08/enzymes-part-2-questions/ Enzymes part 3 http://biochemjm.wordpress.com/2014/03/09/enzymes-part-3-questions/ Biochem JM blog http://biochemjm.wordpress.com/ Biochem JM YouTube http://www.youtube.com/user/BiochemJM
Views: 2072 BiochemJM
Finding Michaelis-Menten constant- CSIR DEC 2017
 
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The Question asked to find Michaelis Menten Constant if graph is plotted against (1/rate) and (1/substrate concentration) and the values of slope and intercepts are given. Question was asked for 4 Marks in DEC 2017 CSIR Exam
Views: 4898 All 'Bout Chemistry
Enzyme Assay
 
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Views: 26888 Purdue Biochemistry
specific activity and turnover
 
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How to calculate the specific activity and turnover of an enzyme
Views: 37808 Peter Klappa
How do you explain Michaelis Menten to a kid?
 
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This video screencast was created with Doceri on an iPad. Doceri is free in the iTunes app store. Learn more at http://www.doceri.com
Views: 37802 Stephen Murata
Enzyme Inhibition (Part 2 of 3) - Noncompetitive Inhibitors
 
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Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam Questions Answered in This Video: - What are noncompetitive inhibitors, and what is mechanism by which they act? - How do noncompetitive inhibitors affect the values of KM and VMAX? - How do noncompetitively inhibited reactions look on the hyperbolic graph and Lineweaver-Burk plot? Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity INFORMATION ABOUT TUTORING: http://www.moofuniversity.com/tutoring/ TO SUPPORT MOOF UNIVERSITY WITH A FINANCIAL CONTRIBUTION: http://www.moofuniversity.com/support-moof/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity Video Content Summary: Noncompetitive inhibitors, unlike competitive inhibitors, do not bind at the active site. They bind a site elsewhere on the enzyme. Thus, they can bind free enzyme OR the enzyme-substrate complex. So, the enzyme-substrate complex, the enzyme-noncompetitive inhibitor complex, and the enzyme-substrate-noncompetitive inhibitor complex can all potentially form. Of course, as long as the noncompetitive inhibitor is bound, the enzyme will not be able to convert substrate into product. Since a noncompetitive inhibitor binds at a site other than the active site and does not have an impact on whether or not substrate can bind, the affinity of enzyme for substrate is not changed, and the KM value remains unchanged. However, the effect of a noncompetitive inhibitor cannot be overcome by increasing substrate concentration, and as long as there are noncompetitive inhibitors present, there will be a smaller number of functional enzymes, relative to an uninhibited case. Less functional enzymes means lower rate of catalysis and a lower VMAX. The effects of a noncompetitive inhibitor on an enzyme-catalyzed reaction are depicted in a variety of ways in the video, and it is shown what happens to the hyperbolic graph and the Lineweaver-Burk plot, otherwise known as the double reciprocal plot.
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