BMS02-1010 Enzyme Kinetics

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BMS02 - Molecules and Cells Flashcards on BMS02-1010 Enzyme Kinetics, created by Evian Chai on 02/05/2020.
Evian Chai
Flashcards by Evian Chai, updated more than 1 year ago
Evian Chai
Created by Evian Chai about 4 years ago
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Question Answer
What is KCat? The turnover number: number of substrate molecules converted to products in a certain amount of time
What is the substrate vs reaction graph? How does it change as the concentration increases Concentration of substrate on the x axis against rxn At low concentrations, substrate proportional to rxn rate: 1st order At high concentrations, rxn rate independent of substrate: 0 order
What is the Michaelis Menton reaction? What do K1, K-1, and K2 stand for? E+S<-->ES-->E+P K1: E+S-->ES K-1: E+S<--ES K2: ES--> E+P
What are 5 assumptions of the Michaelis Menton reaction? 1. [substrate]>>>[enzyme] 2. [ES] doesn't change 3. Initial velocity used 4. P is small enough to be negligible 5. ES<--E+P ignored
What is the Michaelis Menton equation? V= Vmax[S]/Km+[S]
What does Km represent in terms of Vmax? What about affinity? It is the concentration of substrate when Vmax 1/2. A lower Km indicates a higher affinity
K2....K-1 so rxn to E+P neglibale K2<<<<K-1
What is Kd? The dissociation constant of ES aka K2
What do phosphorylases do? Transfer phosphate group from inorganic molecule to molecule
How does protein phosphorylation affect glycogen phosphorylase and glycogen synthase? Phosphorylation activates glycogen phosphorylase and inactivates glycogen synthase
What does phosphatase do? Uses H20 to cleave Phosphate from molecule
On a graph, what does a competitive inhibitor change and not change? What about noncompetitive inhibitor? -Increases Km but not Vmax bc can be overcome -Decreases Vmax but not Km
What is the difference between allosteric and noncompetitive enzymes? Noncompetitive poisons/damages enzyme
What is an example of negative allosteric regulation on phosphofructokinase? ATP/Citrate on Phosphofructokinase As a result, Fructose 6 phosphate does not become Fructose 1,6 biphosphate
What is an example of positive allosteric regulation on pyruvate kinase? Fructose 1,6-biphosphate and phosphoenol pyruvate increase its activity More conversion of phosphoenol pyruvate-->pyruvate as a result
On the Lineweaver Burke plot, the Y intercept represents.... The X intercept represents.... Y intercept: 1/Vmax (changes w allosteric) X intercept: -1/Km (changes w competitive)
What is an example of a isoenzyme? Lactate dehydrogenase- has 4 monomers Each one can be heart/muscle type
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