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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q

Synthase

A

No ATP needed

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2
Q

Phosphatase

A

uses H2O to remove phosphoryl group

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3
Q

Synthetase

A

Requires ATP

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4
Q

Phosphorylase

A

uses Pi to break bond and make phosphorylated product

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5
Q

Oxidase

A

uses O2 as acceptor without adding it to a reaction

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6
Q

Oxygenase

A

1 or 2 O atoms added

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7
Q

Dehydrogenase

A

Electron acceptor in redox reaction (NAD+ and FAD+)

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8
Q

Coenzymes

A

organic molecules required by some enzymes

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9
Q

Cofactors

A

Inorganic substances required for or to increase rate of catalysis

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10
Q

Holoenzyme

A

enzyme + nonprotein

active

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11
Q

Apoenzyme

A

enzyme without nonprotein

inactive

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12
Q

Km

A

amount of substrate needed to reach 1/2 Vmax

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13
Q

Small Km

A

high affinity for substrate

low conc needed to reach 1/2 Vmax

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14
Q

High Km

A

low affinity for substrate

more conc of substrate needed to reach 1/2 Vmax

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15
Q

Relationship of [E] to Vo and Vmax

A

directly related

2E = 2Vo and 2Vmax

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16
Q

1st Order

A

[S] much lower than Km

velocity proportional to [S]

17
Q

0 Order

A

[S] much greater than Km

velocity is constant and equal to Vmax and is independent of [S]

18
Q

Km and Vmax on Lineweaver-Burk

A 
Increase= closer to 0
decrease= further away from 0
19
Q

Irreversible Inhibitor

A

binds E covalently

can only recover E by making a new E

20
Q

Reversible Inhibitor

A

binds E noncovalently

easy recovery of E

21
Q

Suicide Inhibitor E

A

converts inhibitor into a reactive form in active site

22
Q

Competitive Inhibition effect on Vmax and Km

A

no effect on Vmax

Km increases

23
Q

HMG CoA-reductase

A

rate limiting enzyme in cholesterol biosynthesis

24
Q

Statin Drugs

A

structural analogs of HMG- CoA reductase
compete for active site
lower plasma cholesterol levels

25
Q

Noncompetitive Inhibition effect on Vmax and Km

A

Vmax decreased

no effect on Km

26
Q

Effectors

A

bind to allosteric sites noncovalently
multiple subunits
rate limiters

27
Q

Effector effects

A

change affinity of E for S (change Km)
change max catalytic activity (change Vmax)
be negative- inhibit E activity- decrease Vmax/ increase Km
be positive– increase E activity- increase Vmax/ decrease Km

28
Q

Homotropic Effector

A

substrate serves as effector

increase Vmax or decrease Km

29
Q

Heterotropic Effector

A

effector different than substrate

Biochemistry (14 decks)

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