Enzymes Flashcards

1
Q

Amount of product formed per unit time

A

Velocity

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2
Q

The ______is in the linear part of the M-M curve

A

initial velocity

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3
Q

At high concentration of substrate ({S}»Km) the velocity of the reaction is ______–that is constant and independent of ______

A

At high concentration of substrate ({S}»Km) the velocity of the reaction is zero order–that is constant and independent of substrate concentration

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4
Q

At low concentration of substrate ({S}<

A

proportional

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5
Q

When [S] = 0, v=

A

0

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6
Q

When [S] less than Km

A

v=(Vmax / (Km ) * [S]

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7
Q

When [S] is infinite, v=

A

Vmax

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8
Q

When [S] is equal to Km, v=

A

v=1/2(Vmax)

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9
Q

Small Km reflects a _____ affinity of enzyme for the substrate

A

high

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10
Q

Large Km reflects a _____ affinity of enzyme for the substrate

A

low

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11
Q

Michaelis-Menten kinetic analysis:

Does not require ____

A

pure enzyme

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12
Q

TO MEASURE ENZYME use

A

saturating amounts of

substrate (»Km)

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13
Q

TO MEASURE SUBSTRATE

A

use low substrate levels (lower or at the Km)

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14
Q

If there’s more enzyme (Vmax) Km (does/does not) change

A

does not

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15
Q

Also called the “turn-over” number = how many substrate molecules can be used per second

A

Kcat

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16
Q

The Kcat =

A

The Kcat = Vmax/the enzyme concentration

17
Q

LB plot:

X intercept=

A

intercept=-1/Km

18
Q

LB plot:

Y-intercept

A

1/Vmax

19
Q

LB plot:

Slope

A

Km/Vmax

20
Q

Competitive inhibitors bind to

A

binding site only

21
Q

Noncompetitive inhibitors bind to

A

catalytic machinery only

22
Q

Irreversible inhibitors

A

Kill the enzyme

23
Q

Ki

A

inhibitor constant. Inversely related to affinity constant of the inhibitor for the enzyme.

24
Q

The lower the Ki, the ____ it binds

A

The lower the Ki, the tighter it binds

25
Q

Irreversible inhibitors

Example

A

Compound DIFP inhibits serine protease

26
Q

Competitive inhibitors change _____, but not _____

A

change Km, but not Vmax

27
Q

Noncompetitive inhibitors change ____, but not ____

A

change Vmax, but not Km

28
Q

Irreversible inhibitors change ______, but not _____

A

Irreversible inhibitors change Vmax, but not Km

29
Q

5 ways to regulate enzymes

A
1. Regulation by Location
2, Enzyme Zymogens
3. Protein inhibitors
4. Protein phosphorilation
5.Regulation by Substrate Levels
30
Q

Example of: Regulation by Location

A

Enzymes in Blood Plasma: common indicator of liver damage is alanine transaminase (ALT). (A liver enzyme that balances amino acid levels). A high level is indicative of cell damage.

31
Q

Example of: Protein Inhibitors

A

“anti-elastase” in lung tissue.

Oxidized a1-antitrypsin does not effectively inhibit elastase–>Elastase cleaves elastin–>Lung scarring & emphysema

32
Q

The basic concept is that phosphorylation or dephosphorylation modifies the charge of an amino acid residue. If the serine, threonine, or tyrosine is in or near the active site of an enzyme, the enzyme activity may be changed.

A

Protein Phosphorylation

33
Q

Changes in the substrate concentration changes enzyme activity

A

Regulation by Substrate Levels

34
Q

Allosteric enzymes are more sensitive to substrate and (4)

A
  • Usually contain multiple subunits
  • Does not usually follow Michaelis -Menten kinetics; can define an ‘apparent’ Km
  • Usually have binding sites for affector molecules
  • Often regulate a reaction pathway
35
Q

An allosteric enzyme is often at ______

A

at the beginning of a dedicated reaction pathway

36
Q

Allosteric enzymes exist in ___ and ____ forms and

have binding sites for effectors

A

R and T forms

37
Q

_____ is the inhibition of the

product of the reaction

A

Direct product inhibition

38
Q

_______ is

typically the product inhibiting an earlier reaction

A

Feedback inhibition