amino acid biosynthesis Flashcards

1
Q

how many amino acids can we produce (non-essential)

A

10

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2
Q

list the 10 non-essential amino acids

A

alanine, glutamate, glutamine, proline, arginine, serine, glycine, cysteine, aspartate, asparagine

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3
Q

list 3 ways in which amino acids are derived

A

glycolysis intermediates, CAC intermediates, PPP intermediates

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4
Q

describe how amino acids can be derived from the PPP

A

Glucose-6-P can be converted to metabolites by donating electrons to NADP+, producing lots of NADPH

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5
Q

what do aminotransferases do

A

move amino groups from one molecule to another

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6
Q

what is the name of the leftover molecule when an aminotransferase removes it’s amino group

A

carbon skeleton

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7
Q

which amino group was removed to create a carbon skeleton: backbone or R group

A

backbone (because not every a.a has an R group amine)

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8
Q

what is another name (the chemical name) for an amino acid minus its R group

A

a-keto acid

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9
Q

last class we saw that a-KG can make glutamate which can then make glutamine. List the other two derivatives of glutamate (aka a-KG derivatives)

A

proline and arginine

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10
Q

describe how proline is made from glutamate

A

glutamate is reduced by dehydrogenase and NADPH, The resulting molecule is spontaneously (non-enzymatically) cyclized. A final NADPH reduction = proline

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11
Q

to make proline: what enzyme is used

A

glutamate dehydrogenase

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12
Q

to make proline: ATP cost?

A

1 ATP

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13
Q

to make proline: NADPH cost?

A

uses 2 NADPH

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14
Q

describe how you make arginine from glutamate

A

reduce glutamate with NADPH. Aminotransferase introduces a second amino group, leaving glutamate as a-KG. Resulting molecule = ornithine, which enters the urea cycle to form arginine

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15
Q

to make arginine: enzymes used?

A

aminotransferase

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16
Q

to make arginine: ATP cost?

A

2 ATP

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17
Q

to make arginine: NADPH cost?

A

1 NADPH used

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18
Q

to make arginine: what intermediate is produced

A

ornithine

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19
Q

to make arginine: what happens to ornithine during the pathway

A

it enters the urea cycle to eventually form arginine

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20
Q

how many amino groups does arginine have

A

4

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21
Q

how many amino groups does urea have

A

2

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22
Q

what amino acid is produced from 3-phosphoglycerate? what amino acids does that produce?

A

serine, which makes glycine and cysteine

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23
Q

describe how we make serine from 3-phosphoglycerate

A

3-PG is oxidized by NAD+. Aminotransferase adds an amino group. Phosphatase removes the phosphate

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24
Q

to make serine: enzymes used?

A

aminotransferase and phosphatase

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25
Q

to make serine: ATP cost?

A

none

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26
Q

to make serine: byproducts? (ie are the electron carriers oxidized or reduced)

A

NAD+ is used, NADH is produced

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27
Q

describe how glycine is produced from serine

A

hydroxymethyltransferase removed OH and methyl group from serine

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28
Q

to make glycine: enzymes used?

A

hydroxymethyltransferase

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29
Q

to make glycine: ATP cost?

A

none

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30
Q

to make glycine: and electron carriers?

A

none

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31
Q

describe how to make cysteine from serine

A

plants uptake sulfates (SO4 2-) from the soil which are reduced by NADPH to sulfide (S2-). The sulfide is exchanged for the serine OH

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32
Q

to make cysteine: enzymes used?

A

none that are mentioned (S is replaced with OH)

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33
Q

to make cysteine: ATP cost?

A

none

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34
Q

to make cysteine: electron carriers?

A

NADPH used

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35
Q

which amino acid does OAA make

A

aspartate

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36
Q

which amino acid does aspartate make (that we can synthesize)

A

asparagine

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37
Q

which amino acid does pyruvate make (that we can synthesize)

A

alanine

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38
Q

describe how alanine is made from pyruvate

A

pyruvate is transaminated via aminotransferase

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39
Q

describe how aspartate is made from OAA

A

OAA is transaminated via aminotransferase

40
Q

describe how asparagine is made from aspartate

A

aspartate is amidated. Glutamine donates the NH4+. Enzyme used = asparagine synthetase

41
Q

to make asparagine: enzyme?

A

asparagine synthetase

42
Q

to make asparagine: ATP cost?

A

1 ATP used

43
Q

what does ALL stand for

A

acute lymphoblastic leukemia

44
Q

ALL produces an overabundance of _____________

A

immature lymphocytes

45
Q

what does “acute” mean in acute lymphoblastic leukemia

A

cancer progresses rapidly, developing within weeks and becoming possibly fatal within months

46
Q

which enzyme is produced in very little amounts in the malignant lymphocytes in ALL

A

asparagine synthetase

47
Q

synthesis of which amino is blocked during ALL? why? how do people with ALL get this amino acid?

A

synthesis of asparagine is blocked since very little asparagine synthetase is produced in the malignant lymphocytes. They must acquire it from the diet

48
Q

treatment for ALL involves which enzyme

A

asparaginase

49
Q

describe the actions of asparaginase enzyme in ALL treatment

A

the enzyme depletes asparagine in the blood serum, removing the extracellular source of it for these cancer cells = cuts off the asparagine source for the bad cells

50
Q

in ALL treatment, what happens to the cancerous cells once asparaginase removes the extracellular source of asparagine

A

without ability to synthesize Asn and no Asn to utilize from the surrounding serum, the cells die

51
Q

which amino acids are derived from PEP

A

the ringed amino acids: phenylalanine, tyrosine, tryptophan

52
Q

T or F: PEP is the only thing that can make tyrosine

A

false; it can also be made from phenylalanine

53
Q

before making the three ringed amino acids, what does PEP need to make?

A

chorismate

54
Q

describe how chorismate is made from PEP

A

2x PEP (3C) and erythrose 4-phosphate (4C) form 10C chorismate

55
Q

describe how tyrosine is made from chorismate (PEP)

A

a mutase swaps groups off the chorismate ring. the intermediate is then oxidized, decarboxylated, and transaminated

56
Q

describe how phenylalanine is made from chorismate (PEP)

A

a mutase swaps groups off the chorismate ring. The intermediate is then decarboxylated and transaminated

57
Q

formation of which amino acid involves oxidation: tyrosine or phenylalanine

A

tyrosine

58
Q

what amino acid is formed from ribose-5-phosphate

A

histidine

59
Q

what intermediate must be made from ribose-5-P before histidine formation

A

5-phosphoribosyl-1-pyrophosphate (PRPP)

60
Q

how many phosphates does PRPP have

A

3

61
Q

once PRPP is formed from ribose-5-P, describe how histidine is formed

A

histidine is formed from 5 PRPP carbons and 2 oxygens, a nitrogen and carbon from the adenine ring of ATP, a nitrogen from glutamine, and a nitrogen from glutamate

62
Q

list the molecules that contribute atoms to histidine

A

glutamine, PRPP, glutamate, adenine

63
Q

some of the byproducts from histidine synthesis can be used for ___ synthesis

A

purine

64
Q

what type of feedback inhibition regulates amino acid synthesis pathways

A

allosteric feedback inhibition

65
Q

why is allosteric feedback inhibition used to regulate amino acid synthesis pathways

A

to ensure amino acids aren’t made when they’re already in high concentrations

66
Q

why can negative feedback inhibition be problematic

A

problematic when the same intermediate is needed for multiple amino acids, but it’s being inhibited by one product

67
Q

describe how enzyme multiplicity comes into play with a.a synthesis regulation

A

the enzymes in a pathway will have multiple isozymes, and isozymes are inhibited by different molecules in the pathway. This way, inhibition of A1 isozyme by one product reduces overall A activity, but A2 and A3 are still active to make the other products

68
Q

T or F: the effect of enzyme multiplicity inhibitors is cumulative

A

true

69
Q

list 6 amino acid derivatives

A

nucleotides, heme, lignin, auxin, alkaloids, neurotransmitters

70
Q

what is heme a derivative of

A

glycine

71
Q

heme is required for proper function of both ___ and ___

A

hemoglobin and cytochromes

72
Q

heme degrades into __ and __

A

Fe2+ and bilirubin

73
Q

where/in what conditions will heme be degraded into Fe2+ and bilirubin

A

occurs in damaged/dying RBCs in the spleen

74
Q

T or F: bilirubin is insoluble

A

true

75
Q

from the spleen, where does bilirubin travel to

A

liver

76
Q

how does bilirubin travel to the liver

A

bound to serum albumin

77
Q

what happens to bilirubin upon arrival to the liver

A

converts to a water soluble bile pigment in the liver and released into the small intestine

78
Q

what happens to bile pigment once it’s made from bilirubin in the liver and enters the small intestine

A

some of it makes its way to the kidneys and a derivative helps make urine yellow

79
Q

T or F: bilirubin makes urine yellow

A

false; a derivative of bilirubin makes urine yellow

80
Q

T or F: bilirubin makes feces brown

A

false; a derivative makes feces brown

81
Q

describe what happens when you bruise

A

blood vessels in/near the skin burst and the damaged RBCs release heme

82
Q

why do bruises change color

A

occurs as heme loses oxygen

83
Q

describe what happens as bruises change from purple to yellow

A

heme loses oxygen = purple. Heme degrades into an intermediate biliverdin = green, and eventually bilirubin = yellow

84
Q

what happens if bilirubin is in the blood (caused by excess bilirubin)

A

leads to jaundice

85
Q

what is lignin a derivative of

A

phenylalanine and tyrosine

86
Q

what is the role of lignin

A

forms secondary cell walls in plants, large component of wood and bark

87
Q

what is auxin a derivative of

A

tryptophan

88
Q

role of auxin?

A

regulates shoot/fruit/lead growth and helps stems bend towards light

89
Q

what part of the plant secretes auxin

A

the tip of the plant shoot

90
Q

what are flavoured molecules derivatives of

A

phenylalanine and tyrosine

91
Q

what are alkaloids derivatives of

A

phenylalanine and tyrosoine

92
Q

what are alkaloids

A

nitrogenous chemicals formed in plants

93
Q

list 4 alkaloids

A

caffeine, capsaicin, morphine, nicotine

94
Q

what are neurotransmitters derivatives of

A

tyrosine, glutamate, tryptophan, histidine

95
Q

_____ is a key step in most pathways to synthesize NTs

A

decarboxylation

96
Q

list 5 NTs

A

epinephrine, norepinephrine, histamine, serotonin, GABA