lecture_15legge - Enzyme Kinetics Enzyme Kinetics I...

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1 Enzyme Kinetics I 10/15/2009 Enzyme Kinetics Rates of Enzyme Reactions Thermodynamics says I know the difference between state 1 and state 2 and Δ G = (G f -G i ) But Changes in reaction rates in response to differing conditions is related to path followed by the reaction and is indicative of the reaction mechanism!! Enzyme kinetics are important 1. Substrate binding constants can be measured as well as inhibitor strengths and maximum catalytic rates. 2. Kinetics alone will not give a chemical mechanism 2. Kinetics alone will not give a chemical mechanism but combined with chemical and structural data mechanisms can be elucidated. 3. Kinetics help understand the enzymes role in metabolic pathways. 4. Under “proper” conditions rates are proportional to enzyme concentrations and these can be determine “ metabolic problems”. Chemical kinetics and Elementary Reactions Rate Equations Consider aA + bB + • • • + zZ. The rate of a reaction is proportional to the frequency with which the reacting proportional to the frequency with which the reacting molecules simultaneously bump into each other [ ][ ] [ ] z b a Z B A k Rate = The order of a reaction = the sum of exponents Generally, the order means how many molecules have to bump into each other at one time for a reaction to occur. A first order reaction one molecule changes to another A B A A second order reaction two molecules react A + B P + Q or 2A P 3 rd order rates A + B + C P + Q + R rarely occur and higher orders are unknown. Let us look at a first order rate
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This note was uploaded on 02/22/2011 for the course BCHS 3304 taught by Professor Johnson during the Spring '08 term at University of Houston.

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lecture_15legge - Enzyme Kinetics Enzyme Kinetics I...

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