M1 L5

Question 1

Outline the Michaelis-Menten kinetics to describe enzyme rate behavior with respect to substate concentration; including turnover number

Answer 1

E + S ⇌ ES → E+ P
the model for enzyme kinetics relates the reaction velocity V to substrate concentration [S]
Vmax is defined as the max rate in units of concentration/time
Km is defined as the concentration required to reach 1/2 Vmax. hyperbolic curve
V0=Vmax ([S]/[S]+Km)

Question 2

Describe both the kinetics and molecular interaction of the COMPETATIVE inhibition of enzymes. Recognize the inhibition type by its kinetic behavior (V vs [S] plots).

Answer 2

a molecule that can reversibly bind to an enzyme active site but not converted to product
the inhibitor is bound to the enzyme and blocks the substrate from binding, decreases rate of product formation Km increases
separate at the beginning, join at the end curved

Question 3

Describe irreversible enzyme inhibition.

its toxic

Answer 3

irreversible inhibitors bind covalently to their target enzymes, almost all toxic, makes effective inhibitors, good for antibiotic/anti-viral drugs, & makes molecules that are toxic bc they inhibit toxic enzymes

Question 4

Describe both the kinetics and molecular interaction of UNCOMPETATIVE inhibition of enzymes. Recognize the inhibition type by its kinetic behavior

Answer 4

it reversibly binds to the enzyme-substrate complex
decreases both Vmax and Km
start joined, finish apart curved

Question 5

Describe both the kinetics and molecular interaction of MIXED REVERSIBLE inhibition of enzymes. Recognize the inhibition type by its kinetic behavior (V vs [S] plots).

Answer 5

the inhibitor can reversibly bind to both the free enzyme and the enzyme-substrate complex decrease Vmax and increase Km
start joined, finish apart straight