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Biochem > Unit 6 Test Two > Flashcards

Unit 6 Test Two Flashcards

1
Q

Coenzyme of pyruvate dehydrogenase

A

Thiamine pyrophosphate

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2
Q

Coenzyme for lactate dehydrogenase

A

Nicotinamide adenine dinucleotide

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3
Q

Coenzyme of pyruvate carobyxlase

A

Biotin

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4
Q

Coenzyme of methylmalonyl mutase

A

5’-deoxyadenosyl cobalamin

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5
Q

Coenzyme of thymidylate synthase

A

Tetrahydrofolate

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6
Q

Coenzyme of carbonic anhydrase

A

Zn2+

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7
Q

Coenzyme of hexokinase

A

Mg2+

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8
Q

Coenzyme of glutathione peroxidase

A

Se

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9
Q

Coenzyme of superoxide dismutase

A

Mn

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10
Q

Carrier of phosphoryl group

A

ATP

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11
Q

Carrier of electron groups

A

NADH, NADPH, FADH2, FMNH2

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12
Q

Carrier of aldehyde group

A

Thiamine pyrophosphate

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13
Q

Carrier of CO2 group

A

Biotin

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14
Q

Carrier of one-carbon units

A

Tetrahydrofolate

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15
Q

What are the class names of enzymes

A

Oxidoreductase, transferase, hydrolases, Lyases, isomerases, ligases

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16
Q

Examples of oxidoreductase

A

Dehydrogenases, reductases, and oxidases

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17
Q

Examples of transferases

A

Kinases and transaminases

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18
Q

Examples of hydrolases

A

Lipases and proteases

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19
Q

Examples of lyases

A

Anhydrase, dehydratases, and hydratases

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20
Q

Examples of isomerases

A

Isomerases, mutase and epimerases

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21
Q

Examples of ligases

A

Carboxylases and synthetases

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22
Q

What is the vitamin precursor of NADH and NADPH

A

Niacin

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23
Q

What is the vitamin precursor of FADH2 and FMNH2

A

Riboflavin (B2)

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24
Q

What is the vitamin precursor of biotin

A

Biotin

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25
Q

What is the coenzyme of riboflavin

A

FAD

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26
Q

What is the reaction type of riboflavin

A

Redox

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27
Q

What is the coenzyme of pantothenic acid

A

Coenzyme A

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28
Q

What is the reaction type of pantothenic acid

A

Acyl-group transfer

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29
Q

What is the coenzyme of biotin

A

Biocytin

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30
Q

What is the reaction type of biotin

A

Carboxylation and carboxyl synthesis

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31
Q

What are enzymes

A

Catalysts that increase reaction rate without being used up

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32
Q

Most enzymes are

A

Globular proteins

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33
Q

What besides enzymes can also catalyze reactions

A

Ribozymes and some ribosomal RNA

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34
Q

Why is the transition state better than substrate

A

Transition state uses weak non covalent interactions that allow for enzyme and substrate to separate more easily and become products

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35
Q

What is the first # when naming enzymes

A

Defines the class of the enzyme

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36
Q

What is an active site

A

Site where substrate binds to enzyme

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37
Q

What is the nature of active site microenvironment

A

Does not include water unless it is a reactant

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38
Q

Why are cofactors or coenzymes needed

A

Convert apoenzymes to holoenzyme, inactive to active

39
Q

The standard free energy change of a chemical reaction is related to what

A

The equilibrium constant

40
Q

What is the Michaelis complex

A

The non covalent enzyme substrate complex

41
Q

What are the four catalytic mechanisms

A

Acid base catalysis, covalent catalysis, metal ions catalysis, and electrostatic catalysis

42
Q

What is acid-base catalysis

A

Give and take protons

43
Q

What is covalent catalysis

A

Change reaction paths

44
Q

What is metal ion catalysis

A

Use redox cofactors, pKa shifters

45
Q

What are electrostatic catalysis

A

Preferential interactions with TS

46
Q

What are the amino acids which are involved in acid base catalysis

A

Glutamate, aspartate, lysine, arginine, cysteine, histidine, serine and tyrosine

47
Q

What molecules which can act as nucleophile in covalent catalysis

A

Serine, thiolate, amine, and carboxylate

48
Q

How do metal ions assist in enzyme catalysis?

A

Interacts with substrate to facilitate binding, stabilizes negative charges

49
Q

What do you measure in enzyme kinetics

A

Substrate disappearance/ product formation as a function of time (the velocity of a reaction)

50
Q

What is Vmax

A

Maximal velocity when the enzyme is saturated with the substrate

51
Q

What is Km

A

Substrate concentration at which v=1/2 (Vmax)

52
Q

What is the michaelis menton equation

A

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

53
Q

What is saturation kinetics

A

At high substrate concentrations, velocity does not depend on substrate concentration

54
Q

What is the shape of the michaelis menton enzyme kinetic curve

A

Hyperbolic

55
Q

What type of information do you get from MM plot

A

Calculates parameters for Km and Vmax

56
Q

What type of information do you get from linearized double reciprocal plots

A

Analysis of two substrate data or inhibition

57
Q

What type of mechanisms mediate multiple substrate reactions

A

Sequential and ping pong mechanisms

58
Q

What are the factors that affect reaction velocity

A

Substrate concentration, temperature and pH

59
Q

A small Km means what towards affinity

A

High affinity of enzyme for substrate

60
Q

A high Km means what for affinity

A

Low affinity for enzyme and substrate binding

61
Q

What metabolic pathways occur in the mitochondria

A

TCA cycle, fatty acid oxidation and oxidation of pyruvate

62
Q

What mechanisms occur in the cytosol

A

Glycolysis, pentose phosphate pathway, and fatty acid synthesis

63
Q

What mechanisms occur in the nucleus

A

DNA and RNA synthesis

64
Q

What mechanisms occur in the lysosome

A

Degredation of complex macromolecules

65
Q

Do reversible inhibitors stay with enzyme or dissociate

A

Dissociate

66
Q

What is the shape of the allosteric curve

A

Sigmoidal

67
Q

Allosteric enzymes displays what

A

Cooperatively

68
Q

Left shift in the allosteric curve means

A

Positive regulator, high activity R state

69
Q

A right shift of allosteric curve means

A

Negative regulator, curve becomes linear

70
Q

Reversible inhibitors are often used as

A

Drugs

71
Q

What are the three types of inhibition

A

Competitive, uncompetitive and non competitive

72
Q

Where do competitive inhibitors bind

A

To the active site

73
Q

What happens to Vmax or Km of competitive

A

No change in Vmax, increase in Km

74
Q

Does competitive inhibition affect catalysis

A

No

75
Q

What does the uncompetitive inhibitor bind to

A

ES complex

76
Q

Does uncompetitive inhibitors affect catalytic function

A

Inhibits catalytic function

77
Q

What happens to vmax and Km in uncompetitive inhibition

A

Decrease in Vmax, decrease in Km

78
Q

What does the graph look like in uncompetitive inhibition

A

Lines are parallel

79
Q

Is it possible to overcome competitive inhibition

A

Yes by adding more substrate to take the active site over inhibitor

80
Q

What type of inhibitor is pravastatin

A

Competitive

81
Q

Where do noncompetitive inhibitors bind to

A

Other part of enzyme or to ES complex

82
Q

What happens to Km or Vmax of noncompetitive inhbition

A

Vmax decrease only

83
Q

What happens to graph of noncompetitive inhbition

A

Intersect at X axis

84
Q

What is feedback inhibition or end product inhbition

A

Product causes inhibition of the reaction

85
Q

What controls reversible covalent modification

A

Hormones

86
Q

What enzymes are used in reversible covalent modification

A

Kinase and phosphatase

87
Q

What enzymes are used in the irreversible covalent modification

A

Enzymes in gut, like enteropeptidase

88
Q

How are enzymes used as biochemical markers

A

When disease occurs release of enzymes from cells into bloodstream

89
Q

What is the source of ALT, alanine transaminases

A

Liver

90
Q

What marker enzyme is used for hepatitis and cancer

A

ALT, alanine transaminase

91
Q

What marker enzyme is used for muscular dystrophy or MI

A

CPK, creatine phosphokinase

92
Q

What is the source of marker enzymes CPK and creatine phosphokinase

A

Muscle, heart

93
Q

What are the marker enzymes for MI and hepatitis

A

LDH and lactate dehydrogenase

94
Q

What is the source of LDH and lactate dehydrogenase

A

Heart (LDH1) and liver (LDH5)

Biochem (7 decks)

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