7

Question 1

what sites exist for an allosteric enzyme

Answer 1

active and regulatory

Question 2

do allosteric enzymes obey michaelis-menten kinetics

Answer 2

no

Question 3

what kind of activity curves are found for

Answer 3

sigmoidal

Question 4

what is homotropy/homoallosrery

Answer 4

substrates are effectors
may bind active sites or regulatory sitres

Question 5

do allosteric enzymes have quaternary structure

Answer 5

many of them yes

Question 6

describe ATCase

Answer 6

6 catalytic subinits and 6 regulatory
D3 symmetry
first step in CTP biosynthesis
activated by ATP
feedback inhibition

Question 7

what are feedback inhibitors usually

Answer 7

allosteric modulators

Question 8

describe the following as homo/hetero inhibitoris/ activatros for ATc
CTP
ATP
aspratate

Answer 8

CTP heterotropic inhibitor
ATP heterotropic activator
asparate homotropic activator

Question 9

describe the shape of phosphofructokinase

Answer 9

d6 HOMOTETRAMER

Question 10

describe ATP relationship to phosphofructokinase

Answer 10

homotropic inhibitor
2 binding sites (active and regulatory)

Question 11

describe fructose-6-phosphate relationship to phosphofructokinase

Answer 11

binds to active site
homotropic activatro

Question 12

describe AMP relationship to phosphofructokinase

Answer 12

heterotopic(+)

Question 13

describe phosphoenolpyruvate relationship

Answer 13

heterotropic (-)

Question 14

what kind of change is reversible covalent modification associated with

Answer 14

tertriary structure change

Question 15

is glycogen synthase anabolic or catabolic

Answer 15

anabolic

Question 16

how is glycogen phosphorylase reglated

Answer 16

phosphorylation

Question 17

what are phosphrylation sites on glycogen synthase associated with

Answer 17

reducation in actvity

Question 18

is phosphorylate isocitrate dehydrogenase active or inactive

Answer 18

inactive

Question 19

why is phosphorylated isocitrate dehygenase inactiver

Answer 19

phopshate takes same spot as substrate