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Biochemistry > Enzymology > Flashcards

Enzymology Flashcards

1
Q

Turnover rate of an enzyme refers to

A

The fastest speed of an enzym

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2
Q

Enzymes work by reducing

A

Gibbs free energy of activation

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3
Q

Endergonic reactions are_________ and have a ________ G value

A

Non-spontaneous; positive

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4
Q

Exergonic reactions are__________ and have a _______G value

A

Spontaneous; negative

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5
Q

Enzymes do not change the overall Gibbs free energy change for the reaction OR the equilibrium concentrations of substrates and products. T/F

A

True

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6
Q

Hydrolysis of ATP is often used to drive other chemical reactions. T/F

A

True

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7
Q

What are the functions of proteases

A

To break down proteins

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8
Q

What is the function of the hexokinase enzyme

A

To transfer a phosphoryl group

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9
Q

The enzyme chymotrypsin is found where? What is its function

A

Small intestines

Digestive enzyme

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10
Q

The active site of chymotrypsin includes what amino acids?

A

Serine, histidine, and aspartic acid

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11
Q

Cofactors are proteins. T/F

A

False

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12
Q

Cofactors are of two types. What are they?

A

Coenzymes

Metal ions

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13
Q

Cofactors participate in catalysis by

A

Providing functional groups

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14
Q

In humans, cofactors are usually synthesized by

A

Vitamins

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15
Q

What reactions do oxide-reductases catalyze ?

A

Oxidation and reduction reactions

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16
Q

An example of an oxidoreductase is

A

Alcohol dehydrogenase

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17
Q

A common cofactor of alcohol dehydrogenase is

A

NAD+

18
Q

What kind of reaction does transferases catalyze

A

Transfer of C-, N-, or P- containing groups

19
Q

An example of a transferase is_______ and its function is_______

A

Glycerol kinase

To Transfer a phosphate group to glycerol to prepare it for glucose conversion during gluconeogenesis in the liver

20
Q

What reactions do hydrolases catalyze?

A

Catalyze cleavage bonds by adding water

21
Q

examples of a hydrolases include

A

Proteases, esterases, lipases,

22
Q

What reactions do lyases catalyze ?

A

Catalyze cleavage of C-C, C-S, and some C-N bonds

23
Q

What reactions do isomerases catalyze ?

A

Catalyze rearrangements of of isomers

24
Q

What reactions do ligases catalyze

A

Formation of carbon and; O, S and N bonds

Essentially binding of 2 molecules

25
Q

Competitive inhibitors bind to

A

The active site

26
Q

Non-competitive inhibitors bind to

A

Anywhere other than the active site

27
Q

Un-competitive inhibitors bind to

A

Anywhere other than the active site ONLY when the substrate is bound to the enzyme

28
Q

What happens to Vmax and Km during competitive inhibition

A

Vmax remains the same, Km increases.

29
Q

Small Km reflects _______ affinity of enzyme for the substrate

A

High

30
Q

Large Km reflects________ affinity of the enzyme for the substrate

A

Low

31
Q

For Lineweaver-Burk plots, the line representing competitive inhibition_________ on the y-axis with the uninhibited reaction

A

Intersect

32
Q

What happens to Km and Vmax in no competitive inhibition

A

Km stays the same, Vmax decreases

33
Q

What happens to Km and Vmax in uncompetitive inhibition

A

Both decrease

34
Q

Suicide inhibition is when the inhibitor_________bonds to the enzyme and ________the concentration of the enzyme

A

Covalently; reduces

35
Q

What happens to Km and Vmax in suicide inhibition

A

Vmax is decreased, Km stays the same

36
Q

An example of suicide inhibition is

A

Penicillin

37
Q

all enzymes follow Michaelis menten kinetics. T/F

A

False, allosteric enzymes do not

38
Q

How many substrate binding sites do allosteric inhibitors have

A

At least 2

39
Q

Allosteric activators ________ the Km and cause the enzyme to bind to substrate more readily

A

Decrease

40
Q

Allosteric Inhibitors ________ the Km and cause the enzyme to bind less readily to substrate

A

Increase

41
Q

Allosteric activators can only bind to the enzyme when the enzyme is in _____ configuration and inhibitors can only bind the enzym during_____ configuration

A

R; T

Biochemistry (11 decks)

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