7 Flashcards

1
Q

what sites exist for an allosteric enzyme

A

active and regulatory

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2
Q

do allosteric enzymes obey michaelis-menten kinetics

A

no

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3
Q

what kind of activity curves are found for

A

sigmoidal

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4
Q

what is homotropy/homoallosrery

A

substrates are effectors
may bind active sites or regulatory sitres

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5
Q

do allosteric enzymes have quaternary structure

A

many of them yes

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6
Q

describe ATCase

A

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

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7
Q

what are feedback inhibitors usually

A

allosteric modulators

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8
Q

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

A

CTP heterotropic inhibitor
ATP heterotropic activator
asparate homotropic activator

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9
Q

describe the shape of phosphofructokinase

A

d6 HOMOTETRAMER

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10
Q

describe ATP relationship to phosphofructokinase

A

homotropic inhibitor
2 binding sites (active and regulatory)

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11
Q

describe fructose-6-phosphate relationship to phosphofructokinase

A

binds to active site
homotropic activatro

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12
Q

describe AMP relationship to phosphofructokinase

A

heterotopic(+)

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13
Q

describe phosphoenolpyruvate relationship

A

heterotropic (-)

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14
Q

what kind of change is reversible covalent modification associated with

A

tertriary structure change

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15
Q

is glycogen synthase anabolic or catabolic

A

anabolic

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16
Q

how is glycogen phosphorylase reglated

A

phosphorylation

17
Q

what are phosphrylation sites on glycogen synthase associated with

A

reducation in actvity

18
Q

is phosphorylate isocitrate dehydrogenase active or inactive

A

inactive

19
Q

why is phosphorylated isocitrate dehygenase inactiver

A

phopshate takes same spot as substrate