Enzymology Flashcards

(41 cards)

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

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
Competitive inhibitors bind to
The active site
26
Non-competitive inhibitors bind to
Anywhere other than the active site
27
Un-competitive inhibitors bind to
Anywhere other than the active site ONLY when the substrate is bound to the enzyme
28
What happens to Vmax and Km during competitive inhibition
Vmax remains the same, Km increases.
29
Small Km reflects _______ affinity of enzyme for the substrate
High
30
Large Km reflects________ affinity of the enzyme for the substrate
Low
31
For Lineweaver-Burk plots, the line representing competitive inhibition_________ on the y-axis with the uninhibited reaction
Intersect
32
What happens to Km and Vmax in no competitive inhibition
Km stays the same, Vmax decreases
33
What happens to Km and Vmax in uncompetitive inhibition
Both decrease
34
Suicide inhibition is when the inhibitor_________bonds to the enzyme and ________the concentration of the enzyme
Covalently; reduces
35
What happens to Km and Vmax in suicide inhibition
Vmax is decreased, Km stays the same
36
An example of suicide inhibition is
Penicillin
37
all enzymes follow Michaelis menten kinetics. T/F
False, allosteric enzymes do not
38
How many substrate binding sites do allosteric inhibitors have
At least 2
39
Allosteric activators ________ the Km and cause the enzyme to bind to substrate more readily
Decrease
40
Allosteric Inhibitors ________ the Km and cause the enzyme to bind less readily to substrate
Increase
41
Allosteric activators can only bind to the enzyme when the enzyme is in _____ configuration and inhibitors can only bind the enzym during_____ configuration
R; T