micahelis menten kinetics- 13

Question 1

describe zero order kinetics

Answer 1

unimolecular reaction enzyme is saturated

Question 2

Km

Answer 2

Michaelis constant, concentration of substrate where reaction rate is half maximal or half of the active sites are full

Question 3

Vmax

Answer 3

Maximum velocity, maximum rate possible for given concentration of enzyme

Question 4

Kcat

Answer 4

Turnover number, number of substrate molecules converted per active site per time (1st order rate constant)

Question 5

Ks

Answer 5

Dissociation constant for substrate binding

Question 6

Kcat/Km

Answer 6

Specificity constant, measure of enzyme performance by predicting the fate of ES

Question 7

steady state assumption

Answer 7

When substrate concentration is greater than enzyme concentration, entropy is 0, formation of the ES complex occurs at the same rate as its loss

Question 8

when is Vmax reached

Answer 8

Enzyme is fully saturated

Question 9

What is Km relationship to Vmax

Answer 9

Km is reached when Vmax is 1/2

Question 10

What is the rate limiting step of MM

Answer 10

K2

Question 11

What happens when substate concentration is greater than Km

Answer 11

Reached Vmax

Question 12

How can multiple binding site enzymes follow Michealis-Menten kinetics?

Answer 12

Noncooperative

Question 13

How to make Michealis-Menten linear?

Answer 13

Double reciprocal plot (lineweaver-Burk) plot

Question 14

reversible inhibitors

Answer 14

Use noncovalent interactions to bind (competitive, non competitive & uncompetitive)

Question 15

Competitive inhibition Vmax & Km?

Answer 15

Vmax is constant, Km is variable

Question 16

Noncompetitive inhibition Vmax & Km?

Answer 16

Vmax is variable, Km is constant

Question 17

Uncompetitive inhibition Vmax & Km?

Answer 17

Vmax is variable, Km is variable

Question 18

What happens in a bisubstrate reaction in regards to inhibition

Answer 18

The inhibitor is uncompetitive with respect to substrate 1 & competitive with respect to substrate 2

Question 19

What are the 3 assumption made by MM kinetics

Answer 19

binding of the substrate to the enzyme is at equilibrium
since we are measuring initial rate, second step is irreversible
steady state assumption

Question 20

Which are allosteric inhibitors? (2)

Answer 20

Non competitive & uncompetitive

Question 21

graph for 1st order reaction

Answer 21

draw and check

Question 22

graph for 2nd order reaction

Answer 22

draw and check

Question 23

graph for zero order reacrion

Answer 23

draw and check