Biochem Midterm

Front 1

a compound that decreases reaction velocity by binding to the enzyme

Back 1

an inhibitor

Front 2

not covalently bound, is able to dissociate from the enzyme

Back 2

reversible

Front 3

reacts with the enzyme via covalent bonds which lead to permanent loss of activity

Back 3

irreversible

Front 4

for reversible inhibition, what are the four categories?

Back 4

1. competitive 2. noncomp 3. uncompetitive 4. distinguishable by lab kinetics

Front 5

for nonallosteric enzymes, what does competitive inhibition do and how does it effect the km and Vmax levels.

Back 5

competes for binding site. looks like substrate. increases km. Vmax remains the same

Front 6

for nonallosteric enzymes, what does noncompetitive inhibition do, how does it effect the km and the Vmax levels

Back 6

the inhibitor binds at a site other than that active site. Km remains the same, Vmax is lowered

Front 7

for nonallosteric enzymes, what does uncompetitive inhbition do, how does it effect the km and the Vmax levels

Back 7

only binds to the ES to shape the reaction and no product is formed. Km and Vmax decrease

Front 8

this type of allosteric inhibition can over come inhibition by increasing substrate inhibition

Back 8

competitive

Front 9

name an example of a competitive inhibitor

Back 9

succinic acid and malonic acid

Front 10

for enzyme-inhinitor interaction. Ki = [E][I] / [EI] what does Ki stand for?

Back 10

ki = the dissociation constant for the complex

Front 11

what type of nonallosteric inhibition produces a change in conformation of E and decreases in activity. It is similar to the structure of the substrate

Back 11

noncompetitive inhibition. the reaction pathway also includes an ESI complex

Front 12

what type of nonallosteric inhibition is not well characterized kinetically and the inhibitor binds only to the ES complex

Back 12

uncompetitive inhibition

Front 13

product inhibition

Back 13

decreases the rate of a reaction due to the accumulation of a product. its reversible. its means of regulation of a pathway end product inhibition

Front 14

name some examples of nonallosteric irreversible inhibition

Back 14

organo P toxins, nerve gas (Sarin), malathion

Front 15

what are irreversible inhibitions for nonallosteric enzymes

Back 15

COVALENT BOND between inhibitor and a functional group at the active site.
inhibit acetyl-cholin-esterase (essential ser) leads to paralysis and death

Front 16

what type of inhibition does toxicity occur due to tight bonding to functional groups at the active site.

Back 16

heavy metal inhibition

Front 17

this type of inhibition binds a compound to E and is then converted to an active form. The active form then covalently modifies a function group of E

Back 17

suicidal inhibition

Front 18

Name some examples of suicidal inhibition

Back 18

penicilli- its converted to the active form by bacterial enzyme.
Transpeptidase - become deactivated

Front 19

this type of inhibition is nonspecific. HG bonds to many different enzymes - SH of cysteine.

Back 19

heavy metal inhibition

Front 20

what does heavy metal inhibition of nonallosteric enzymes irreversible inhibition effect?

Back 20

it effects the proportional to dosage.