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MCAT BIochem > Enzymes > Flashcards

Enzymes Flashcards

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MCAT flashcards
1
Q

Enzyme

A

Biological catalyst

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2
Q

Does a catalyst change the kinetics or thermodynamics (Delta H) of a reaction?

A

Delta H

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3
Q

What doesnt a catatlyst change?

A

Delta H
Equilibrium constant
Delta G/Free Energy

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4
Q

What does a catalyst change?

A

Lowers the free energy of activation

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5
Q

Enzyme suffix

A

-ase

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6
Q

Oxidoreductase

A

Catalyze oxidation-reduction reactions - transfer of electrons between biological molecules
Often have cofactors that carry electrons ( NAD+ or NADP+)

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7
Q

Reductant

A

Electron donor

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8
Q

Oxidant

A

Electron acceptor

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9
Q

What kind of enzymes are oxidoreductase?

A

Dehydrogenase, reductase, oxidase

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10
Q

Transferase

A

Catalyze the movement of a functional group from one molecule to another

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11
Q

What kinds of enzymes are transferase?

A

aminotransferases, kinases

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12
Q

Example of aminotransferase:

A

aspartate & a-ketoglutarate –>glutamate & oxaloacetate

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13
Q

Kinase

A

Cataylze transfer of phosphate to another molecule

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14
Q

Hydrolase

A

Catalyze breaking of a compound into two molecules using the addition of water

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15
Q

What kinds of enzymes are hydrolase?

A

Phosphatase, Peptidases, nuclease, lipases

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16
Q

Lyase

A

Catalyze the cleavage/synthesis of a single molcule into two products
Do not use water & don’t reduce/oxidizae
Often create double or cyclic bonds

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17
Q

What kinds of enzymes are lyases?

A

Lyase, synthase

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18
Q

Isomerase

A

Rearrange bonds within a molecule

Between stereoisomers & constitiutional isomers

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19
Q

Ligases

A

Catalyze addition or synthesis reactions between large, similar molecules
Requires ATP
Nucleic aid synthesis & repair

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20
Q

Enyzme Type Mnemonic

A

LI’L HOT

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21
Q

Endergonic reaction

A

Requires energy

Delta G > 0

22
Q

Exergonic reaction

A

Spontaneous

Delta G < 0

23
Q

Apoenzyme

A

Enzymes without cofactors

24
Q

Holoenzymes

A

Enzymes with cofactor

25
Q

Prosthetic groups

A

Tightly bound cofactors necessary for enzyme function

26
Q

Cofactor

A

Generally inorganic molecules or metal ions (dietary minerals)

27
Q

Coenzymes

A

Small organic groups that are vitamins or derivatives of vitamins (NAD+, FAD+, coenzyme A)

28
Q

Saturation

A

When an enzyme is working at max velocity and cannot be increased by adding more substrate

29
Q

Michaelis-Menton Equation

A

v=Vmax [S]/Km + S

30
Q

Km

A

Michaelis constant-Substrate concentration at which half of the enzyme’s active sites are full

31
Q

Km can used as a measure of

A

affinity of an enzyme for a substrate
Higher Km=lower affinity
Cannot be altered by concentration

32
Q

What is the slope of a Lineweaver-Burke plot

A

Km/Vmax

33
Q

What is the y-intercept of Lineweaver-Burke plot

A

1/Vmax

34
Q

What is the x-intercept of Lineweaver-Burke plot

A

-1/Km

35
Q

What does as sigmoidal shape on a Michaelis-Menton plot mean?

A

Cooperativity

36
Q

Why is there a sigmoidal shape in cooperativity?

A

As one subunit is bound with substrate, the next subunit has a more increased likelihood of wanting that conformation as well

37
Q

What things mainly affect enzyme activity/rate/velocity

A

pH, temperature & salinity

38
Q

Optimal human body temperature

A

98.6 F or 37 C

39
Q

Affect of temperature on enzymes

A

Activity increases every 10 C, until optimal temperature

40
Q

Optimal blood

A

pH 7.4

41
Q

What does a competitive inhibitor do to the Km value?

A

Increases it because more substrate will be needed to reach half the maximum velocity

42
Q

What does competitive inhibitor do to Vmax value?

A

Nothing, same y-intercept

43
Q

What does a noncompetitive inhibitor do to Vmax?

A

Decreases it because there is less enzyme available to react

44
Q

What does a noncompetitive inhibitor do to Km?

A

Doesnt change, any copies of enzyme still maintain same affinity for substrate

45
Q

Mixed inhibition

A

Inhibitor can bind to enzyme or enzyme-substrate complex

Binds at allosteric site

46
Q

Mixed inhibition affects:

A

Km:
Binds to enzyme- increases Km (lower affinity)
Binds to enzyme-substrate complex- lowers Km (higher affinity)
Vmax decreases

47
Q

Uncompetitive Inhibition

A

Bind only to enzyme-substrate complex and lock them together

Bind at allosteric site

48
Q

Uncompetitive inhibition affects:

A

Lower Km & Vmax

49
Q

Allosteric Enzyme

A

Have active & allosteric sites that have allosteric inhibitors or activatoirs

50
Q

Zymogen

A

Secreted inactive and contain catalytic domains &regulatory domains to turn themselves on/off

51
Q

Velocity of the reaction rate equation

A

v= vmax[S]/Km + [S}

MCAT BIochem (8 decks)

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