Learn: exam 3 pt 2

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75 Terms

1
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What substrate enters the oxidative PPP?

Glucose-6-phosphate.

2
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What does the oxidative PPP generate?

NADPH and ribulose-5-phosphate, releasing CO₂.

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What is the purpose of the nonoxidative PPP?

Reversible sugar-phosphate rearrangements.

4
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Which glycolytic intermediates connect to the PPP?

Fructose-6-phosphate and GAP.

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Can the nonoxidative PPP run in reverse?

Yes.

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Which pathway produces ribose-5-phosphate?

Pentose phosphate pathway.

7
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Why do muscles convert pyruvate to lactate anaerobically?

Regenerate NAD⁺ for glycolysis.

8
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Why do yeast convert pyruvate to ethanol anaerobically?

Regenerate NAD⁺ for glycolysis.

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Does fermentation require oxygen?

No.

10
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What happens if NAD⁺ becomes unavailable to GAPDH?

Glycolysis stalls at GAPDH.

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What is the Warburg effect?

High glycolysis rates in cancer cells, even with oxygen present.

12
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What does a radiolabeled hydrogen on GAP C1 become during GAPDH?

Part of NADH.

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What does PDH convert pyruvate into?

Acetyl-CoA, CO₂, and NADH.

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Where is PDH located?

Mitochondrial matrix.

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Is PDH one enzyme or a multienzyme complex?

Multienzyme complex.

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What does PDH E1 use?

TPP.

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What does PDH E2 use as its swinging arm?

Lipoamide.

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What does PDH E3 do?

Reoxidizes reduced lipoamide via FAD and NAD⁺.

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What is the net reduced cofactor leaving PDH?

NADH.

20
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What is substrate channeling?

Direct intermediate transfer between active sites.

21
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Why is substrate channeling useful?

Limits intermediate loss and side reactions.

22
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What does alanine scanning test?

Importance of individual amino acid residues.

23
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How do you perform an alanine-scanning experiment?

Mutate a selected residue to alanine and measure enzyme activity.

24
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What does loss of activity after mutation suggest?

Original residue is important for enzyme function.

25
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What does radioactive labeling test?

Where a specific atom travels through a reaction.

26
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What does stereospecificity mean?

Enzyme selectively reacts with or produces a particular stereoisomer.

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92. What does ΔG < 0 mean?

Forward reaction is thermodynamically favorable.

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93. What does ΔG > 0 mean?

Forward reaction is thermodynamically unfavorable.

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94. What does ΔG = 0 mean?

Equilibrium.

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95. What does negative ΔG°′ imply about Keq?

Keq > 1.

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96. What does positive ΔG°′ imply about Keq?

Keq < 1.

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97. What is Q?

Products/reactants, with stoichiometric exponents.

33
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98. What happens when Q < Keq?

Forward reaction is favorable.

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99. What happens when Q > Keq?

Reverse reaction is favorable.

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100. If actual ΔG is more negative than ΔG°′, what does that imply?

Q < 1; reactants favored in the concentration ratio.

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101. When calculating Keq from ΔG°′, what mathematical operation isolates Keq?

Exponentiate after dividing by −RT.

37
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102. What units must temperature use?

Kelvin.

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103. What units must match when using R?

ΔG and R must use compatible energy units.

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104. How do you identify the electron acceptor?

Species being reduced (gains electrons).

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How do you identify the electron donor?

Species being oxidized (loses electrons).

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What direction is spontaneous electron transfer?

Lower to higher reduction potential.

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107. What does positive ΔE°′ imply?

Negative ΔG°′; favorable standard redox reaction.

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108. What does negative ΔE°′ imply?

Positive ΔG°′; unfavorable standard redox reaction.

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109. In a redox calculation, what does n represent?

Number of electrons transferred.

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110. If [reduced]/[oxidized] increases, what happens to reduction potential?

It decreases.

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111. Does a reaction with positive ΔG°′ always have positive actual ΔG?

No; concentrations can make actual ΔG negative.

47
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112. If an enzyme is inhibited, what often happens to its substrate?

It accumulates.

48
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113. If an enzyme is inhibited, what often happens to downstream products?

Their production decreases.

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114. Can a favorable reaction drive an unfavorable one?

Yes, through reaction coupling.

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115. What is the difference between ΔG and ΔG°′?

Actual cellular conditions vs. biochemical standard conditions.

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116. Does a catalyst change Keq or ΔG?

No; it changes reaction rate.

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117. What happens when a pathway's final product inhibits its first committed step?

Pathway flux decreases.

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118. Does an enzyme's stereospecificity mean it makes equal amounts of stereoisomers?

No; it favors a specific stereoisomer.

54
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119. If the reduced form of a redox cofactor accumulates, what happens to its reduced/oxidized ratio?

It increases.

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120. What does a strongly negative ΔG tell you about reaction direction?

Forward direction is favorable under those conditions.

56
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Which polysaccharide is a homopolymer of D-glucose?

Cellulose; β(1→4) bonds.

57
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What is chitin made of?

N-acetylglucosamine; β(1→4) bonds.

58
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Where is chitin commonly found?

Insect exoskeletons.

59
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What are glycosaminoglycans (GAGs) made of?

Repeating disaccharides.

60
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Why are GAGs negatively charged?

Sulfate and carboxylate groups.

61
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What is peptidoglycan made of?

NAG + NAM with peptide crosslinks.

62
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Where is peptidoglycan found?

Bacterial cell walls.

63
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What bonds does amylose contain?

Unbranched α(1→4) glucose bonds.

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What bonds does amylopectin contain?

α(1→4) chains and α(1→6) branches.

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What makes glycogen different from amylose?

Glycogen is highly branched.

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How many electrons does NADH transfer?

2 electrons; water-soluble cosubstrate.

67
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How many electrons does NADPH transfer?

2 electrons; water-soluble cosubstrate.

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How many electrons can FAD transfer?

1 or 2 electrons; enzyme-bound prosthetic group.

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How many electrons can FMN transfer?

1 or 2 electrons; enzyme-bound prosthetic group.

70
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How many electrons can ubiquinone (Q) transfer?

1 or 2 electrons; lipid-soluble mobile carrier.

71
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How many electrons does cytochrome c transfer?

1 electron; water-soluble mobile protein.

72
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How many electrons do Fe-S centers transfer?

1 electron; protein-bound prosthetic groups.

73
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How many electrons does cytochrome heme transfer?

1 electron at a time; protein-bound prosthetic group.

74
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Which electron carrier moves within the lipid membrane?

Ubiquinone (Q/QH₂).

75
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What is the net mobile reduced product of succinate dehydrogenase?

QH₂; FAD remains enzyme-bound.