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Biochem-Enzymes 3

Med’11 Biochemistry Enzymes

What is enzyme kinetics? Study of the rates of enzyme-catalyzed reactions
What is the velocity of a reaction? The rate of catalysis, defined as the number of moles of product formed per second
What is the initial velocity of a reaction? Measured at the very beginning of a reaction when very little P has been made. It depends on the amount of substrate present
What is the turnover number (Kcat)? The number of substrate molecules converted to product per enzyme molecule per unit of time, when E is saturated with substrate (μmol/ min/ mol of enzyme). It is a measure of catalytic activity.
What happens to enzyme concentration and initial velocity when substrate concentration is very high? Enzyme concentration: approaches 0 Initial velocity: approaches maximum velocity
What factors affect enzyme reactivity? Substrate concentration pH Temperature
On what assumptions is the Michaels-Mentin equation built? ES is formed ES in rapid equilibrium with free E Rate of E+P formation is less than rate of ES formation and E+S formation.
What is the Michaels-Mentin equation? Vmax [S] V = ________ Km + [S]
Describe Vmax. Constant Theoretical, never achieved in reality To be achieved, ALL enzymes must be bound to substrates. V approaches Vmax as substrate concentration increases
Describe the kinetic activator constant (Km) Constant Derived from rate constants Under Michaels-Mentin conditions, is the ES dissociation constant Small Km: tight bonding Large Km: weak bonding
What is the equation for Km? Km = (K2 + K3) / K1
What is the shape of the graph of the Michaels-Mentin equation? Rectangular hyperbola
What is the relationship between the Michaels-Mentin equation and the Lineweaver-Burk equation? The LBE is a double reciprocal equation of the MME so as to give a linear graph to correctly identify the Km and Vmax
Created by: Salma O
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