1Enzyme Kinetics
helps us understand how enzymes work and reveals how reglutory ligands such as activators and inhibitors work
2Intitial Rate Definition
# of moles of product formed per second (at 0)
3Michaelis Menten Equation
V0= vmax(s)/Km+ (s)
4Binding Step
forward is K1, backward is K2
E+S=ES
5Catalytic step
kCat(turnover number0 and this is only forward
ES=E+P
6We assume that ES is _______ in the Michaelis Menten Equation
constant
7Michaelis Constant formula
Km=k-1+kcat/k1
8The substrate as Y and X
Y=1/(v0) X= 1/(s)
9Enzymes with Km much lower allow the enzyme to operate at ____________ rate, independent of small fluctuations. The enzyme will ________ be saturated with substrate.
maximum, always
reverse is true as well
11Km
substrate concentration that is needed to achieve half of Vmax
12Kcat
turnover number and denotes how fast a bound substrate is processed by an enzyme.
13Kcat/Km
catlytic efficency
14Catlytic perfection
every collision is limited by the frequency of collision between enzymes and its substrate