ch18 nitrogen metabolism

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101 Terms

1
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Nitrogen metabolism primarily focuses on which element’s fate in the body?

Nitrogen

2
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Nitrogen is essential for all of the following EXCEPT:

Anything other than amino acids, nucleotides, or coenzymes

3
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What is the major reason nitrogen metabolism must be tightly regulated?

Ammonia toxicity

4
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Approximately what percentage of the Earth’s atmosphere is N₂?

78%

5
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Humans cannot directly use atmospheric N₂ because:

Humans cannot take nitrogen from the atmosphere and rely on bacteria to process it

6
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Nitrogen fixation is carried out primarily by:

Nitrogen-fixing bacteria

7
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In plants, nitrogen-fixing bacteria are commonly found:

In the roots

8
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“Fixing” nitrogen refers to:

Converting atmospheric nitrogen to a usable biological form

9
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The enzyme responsible for reducing atmospheric N₂ to NH₃ is:

Nitrogenase

10
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Nitrogenase-catalyzed nitrogen fixation:

Produces ammonia (NH₃)

11
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Nitrogenase requires which of the following conditions?

Anaerobic conditions

12
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The nitrogenase reaction is energetically:

Energy-demanding (requires 16 ATP)

13
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Which enzyme converts glutamate to glutamine by adding an extra amino group?

Glutamine synthetase

14
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Glutamine can be described as an “ammonia sponge” because it:

Stores an extra amino group and safely carries ammonia

15
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Nitrogen enters most biological molecules primarily in the form of:

Amino groups (–NH₂)

16
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The enzyme that converts glutamine + α-ketoglutarate into 2 glutamate is:

Glutamate synthase

17
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In the glutamate synthase reaction, which TCA intermediate is used as a carbon skeleton?

α-ketoglutarate

18
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Together, glutamine synthetase and glutamate synthase accomplish:

Assimilation of NH₄⁺ into organic molecules

19
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Transaminases (aminotransferases) catalyze reactions that:

Transfer amino groups between molecules

20
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Transamination reactions are important because they:

Link amino acid and keto acid pools through reversible reactions

21
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A typical transamination reaction involves:

Reversible transfer of amino groups between amino acids and keto acids

22
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Transaminations are highly regulated because:

Ammonia is toxic

23
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The main “amino group donor” in many transamination routes is:

Glutamate

24
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Which statement best describes glutamine’s role in nitrogen metabolism?

A safe, non-toxic carrier and storage form of nitrogen

25
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The major reason the body uses organic carriers instead of free NH₃ is to:

Prevent ammonia toxicity

26
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Which pair represents the interconversion central to nitrogen assimilation?

Glutamate ↔ α-ketoglutarate

27
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Which molecule is both a TCA intermediate and central in nitrogen assimilation?

α-ketoglutarate

28
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The main metabolic danger of elevated glutamine in the brain is:

Cerebral edema

29
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Which statement about nitrogen acquisition and disposal is TRUE?

Nitrogen acquisition + nitrogen disposal (urea cycle)

30
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The urea cycle is most directly linked to nitrogen:

Nitrogen disposal

31
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Amino acids are derived mainly from intermediates of:

Glycolysis, TCA cycle, pentose phosphate pathway

32
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The primary nitrogen sources for amino acid biosynthesis are:

Glutamate and glutamine

33
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Essential amino acids are those that:

Must be obtained from the diet

34
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Nonessential amino acids:

Are synthesized by the body

35
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The glutamate family of amino acids is grouped because they:

Share a 5-carbon backbone

36
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Serine can serve as a precursor for:

Glycine

37
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Folate is important in amino acid metabolism because it:

Carries out one-carbon transfers

38
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Folate has a critical role in:

One-carbon transfers and purine synthesis

39
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Essential amino acid synthesis pathways are often:

Long and energy-intensive

40
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Humans do not synthesize sulfur-containing amino acids because:

We cannot efficiently incorporate sulfur

41
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The branched-chain amino acids include:

Valine, leucine, isoleucine

42
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The aromatic amino acids include:

Phenylalanine, tyrosine, tryptophan

43
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Histidine is synthesized from:

ATP + PRPP

44
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Glutamate, GABA, and glycine are all:

Neurotransmitters

45
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GABA is produced from which amino acid?

Glutamate

46
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The enzyme that converts glutamate to GABA is:

Glutamate decarboxylase

47
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GABA’s principal effect in the nervous system is to:

Prevent overstimulation

48
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Drugs like benzodiazepines act by:

Enhancing GABA’s inhibitory action

49
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Catecholamines dopamine, norepinephrine, epinephrine are derived from:

Tyrosine

50
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Parkinson’s disease is primarily associated with deficiency of:

Dopamine

51
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A common treatment for Parkinson’s disease involves:

Dopamine agonists

52
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Serotonin and melatonin are synthesized from:

Tryptophan

53
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Prozac (fluoxetine) is best described as a:

Serotonin reuptake inhibitor

54
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Amino acids can be used as metabolic fuel primarily in:

Small intestine and liver

55
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Amino acid catabolism usually begins with:

Transamination

56
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After transamination, the carbon skeleton of amino acids:

Enters TCA, gluconeogenesis, or ketogenesis

57
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A glucogenic amino acid yields:

TCA cycle intermediates → glucose

58
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A ketogenic amino acid yields:

Acetyl-CoA or acetoacetate

59
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Ketosis occurs when:

Sugar is low and ketones become major fuel

60
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Phenylketonuria (PKU) is characterized by:

Accumulation of phenylalanine

61
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A key clinical feature of untreated PKU is:

Neurological impairment

62
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PKU is typically managed by:

A low-phenylalanine diet

63
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The main physiological purpose of the urea cycle is to:

Detoxify ammonia → urea

64
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The urea cycle occurs primarily in:

Liver

65
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The committed enzyme of the urea cycle is:

Carbamoyl phosphate synthetase I (CPS I)

66
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Carbamoyl phosphate synthetase I is located in the:

Mitochondria

67
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The first step of the urea cycle incorporates ammonia into:

Carbamoyl phosphate

68
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In the liver, toxic ammonia is first handled in the:

Mitochondria

69
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The ornithine–citrulline antiporter:

Moves ornithine in and citrulline out

70
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N-acetylglutamate (NAG) regulates the urea cycle by:

Activating CPS I

71
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A nucleotide is composed of:

Base + sugar + phosphate

72
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A nitrogenous base attached only to a sugar is called a:

Nucleoside

73
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Purine bases include:

Adenine and guanine

74
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Pyrimidine bases include:

Cytosine, uracil, thymine

75
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Purines are structurally characterized by:

A two-ring structure

76
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Pyrimidines are structurally characterized by:

A one-ring structure

77
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“Pure As Gold” refers to:

Purines = A, G

78
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“CUT the PY” refers to:

Pyrimidines = C, U, T

79
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In RNA, the sugar is:

Ribose

80
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In DNA, the sugar is:

Deoxyribose

81
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The phosphate attaches to which carbon?

Carbon 5

82
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Thymine is found mainly in:

DNA

83
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Uracil is found mainly in:

RNA

84
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DNA uses thymine instead of uracil because:

Allows detection of cytosine deamination

85
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Which base pair forms two hydrogen bonds?

A–T

86
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Which base pair forms three hydrogen bonds?

G–C

87
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Nucleotides function as all EXCEPT:

Structural lipids

88
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cAMP and cGMP function as:

Second messengers

89
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In de novo purine synthesis, the ring is:

Built onto ribose (PRPP)

90
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Amino acid precursors for purine synthesis include:

Glycine, glutamine, aspartate

91
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The common purine precursor for AMP and GMP is:

IMP

92
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Conversion of IMP to AMP uses:

GTP

93
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Conversion of IMP to GMP uses:

ATP

94
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In pyrimidine synthesis, the ring is:

Built first, then attached to ribose

95
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Primary precursors for pyrimidine synthesis include:

Aspartate, carbamoyl phosphate, CO₂

96
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Ribonucleotide reductase converts:

Ribonucleotides → deoxyribonucleotides

97
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Ribonucleotide reductase is allosterically regulated by:

ATP activates, dATP inhibits

98
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Thymidylate synthase converts:

dUMP → dTMP

99
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The methyl donor used by thymidylate synthase is:

THF

100
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Purines degrade to:

Uric acid

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