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Biochemistry II > Unit II Amino Acid Metabolism > Flashcards

Unit II Amino Acid Metabolism Flashcards

1
Q

With a low energy charge what will happen to an amino acid?

A

it is oxidized to get ATP

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2
Q

With low blood glucose, what will happen to an amino acid?

A

it’s converted to eneter gluconeogenesis to get glucose

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3
Q

What will happen to amino acid with a high energy charge and lots of glucose?

A

it’s converted in the liver for fat synthesis to make fat

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4
Q

Can amino acids be stored?

A

no

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5
Q

If an AA can’t be stored then what happens to it?

A

its broken down (catabolism)

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6
Q

What group is removed from an AA during catabolism?

A

an amino group

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7
Q

If an amino group is removed from an alpha carbon on an AA, what is produced?

A

alpha-ketoglutarate acid

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8
Q

What is the final product of amino acid catabolism when removing the amino group?

A

urea

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9
Q

What are the final products of AA catabolism when creating an alpha-keto acid?

A

ATP, Glucose, and Fatty acids

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10
Q

What is the main site for AA catabolism?

A

the liver

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11
Q

What does 50% of ATP production in the liver come from?

A

AA oxidation

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12
Q

Where are branched chain AA’s more often catabolized?

A

skeletal and cardiac muscle

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13
Q

What are the branched chain AA that the skeletal muscle is able to oxidize?

A

Leucine, Isoleucine, and Valine (LIV)

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14
Q

What are the other AA’s that skeletal muscle can oxidize?

A

Glutamate, Aspartate, and Asparagine (GAA)

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15
Q

All together what are the six AA’s that can be oxidized in the muscle?

A

LIV GAA

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16
Q

What is transamination?

A

the transfer of an amino group from one AA to an alpha-keto acid

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17
Q

What is deamination?

A

the removal of an amino group from an AA

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18
Q

What type of enzyme is associated with transamination?

A

aminotransferases, transaminases

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19
Q

What type of enzyme(s) is/are associated with deamination?

A

lyases, dehydratases, or dehydrogenases

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20
Q

What coenzyme is required for transamination?

A

pyridoxal phosphate

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21
Q

List some examples of aminotransferases

A

Alanine aminotransferase, and aspartate aminotransferase

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22
Q

What would be the result of an AA transfering its alpha-amino group to alpha-ketoglutarate?

A

glutamate and alpha-keto acid

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23
Q

Are transaminations reversible?

A

yes

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24
Q

In the oxidative demaination of glutamate, what would be the products?

A

alpha-ketoglutarate and and free ammonia

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25
Q

What is the enzyme used to deaminate glutamate?

A

glutamate dehydrogenase

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26
Q

What cofactor is coupled with glutamate dehydrogenase?

A

NAD+

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27
Q

What are alpha-keto acids also known as?

A

carbon skeletons

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28
Q

What are some examples of pathways that an alpha-keto acid may enter?

A

krebs, gluconeogenesis, and fat synthesis

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29
Q

What is the fate of ammonia?

A

excretion as urea

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30
Q

What is the alpha-ketoacid of alanine?

A

pyruvate

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31
Q

What is the alpha-ketoacid of aspartate?

A

oxaloacetate

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32
Q

What is the alpha-ketoacid of glutamine?

A

alpha-ketoglutarate

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33
Q

What is the alpha-ketoacid of glutamate?

A

alpha-ketoglutarate

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34
Q

How does an amino group make it into the mitochondria?

A

attached to glutamate

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35
Q

Once an amino group is in the mitochondria as glutamate, what then happens to that amino group?

A

it is excreted or transfered to an alpha-ketoglutarate to be used in other metabolic pathways

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36
Q

Ammonia in extrahepatic tissues is transported to the liver in what form?

A

glutamine

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37
Q

What enzyme is used to stick an extra amino group on glutamate?

A

glutamine synthetase

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38
Q

Does glutamine synthetase require energy?

A

yes, ATP

39
Q

How is muscle a nitrogen donor?

A

by stealing amino groups, taking their nitrogen, and creating glutamine

40
Q

What enzyme in the muscle turns glutamate into glutamine?

A

glutamine synthase

41
Q

What does glutamine synthase add ti glutamate in the muscle?

A

nitrogen

42
Q

In the muscle, what turns glutamine back to glutamate?

A

glutaminase

43
Q

What is the alpha-ketoacid of alanine?

A

pyruvate

44
Q

In skeletal muscle, what makes alanine from pyruvate?

A

alanine aminotransferase (ALT) or glutamate-pyruvate transaminase (GPT)

45
Q

In exercising muscle a lot of pyruvate is created, what would this push the reaction towards?

A

the making of alanine

46
Q

In the liver a lot of alanine is coming skeletal muscle, what would this push the reaction towards?

A

making pyruvate

47
Q

What enzyme transfers an amino group from glutamate to oxaloacetate to make aspartate?

A

aspartate aminotransferase (AST) or glutamate oxaloacetate transaminase (GOT)

48
Q

What transport shuttle is aspartate used in?

A

the malate-aspartate shuttle system

49
Q

What is the nitrogen from aspartate donatedto?

A

for purines/pyrimidine synthesis or used inthe urea cycle

50
Q

If nitrogen isn’tbeing usedfor synthesis,what happens to it?

A

it is excreted through to urea cycle

51
Q

List a couple of reasons why liver may be getting lost of nitrogen

A

Eaten to much protein, GNG, exercise, starvation, and no carbs in diet

52
Q

Glutamine can transfer nitrogen to the liver, what enzyme places an amino group on glutamate to make it into glutamine?

A

glutamine synthase

53
Q

Besides glutamine, what else can transport nitrogen to the liver?

A

alanine-glucose cycle

54
Q

What does the first NH3 on urea come from?

A

from glutamate dehydrogenase (GDH)

55
Q

How does glutamate dehydrogenase create an amino group?

A

via oxidatative deamination of glutamate

56
Q

Where does the second NH3 on urea come from?

A

from aspartate aminotransferase (AST)

57
Q

How does AST create an amino group for urea?

A

it transfers amino groups from glutamate to oxaloacetate, which forms aspartate

58
Q

What is the alpha-ketoacid of glutamate again?

A

alpha-ketoglutarate

59
Q

What enzyme would create carbamoyl phosphate from CO2, NH3, and 2 ATP?

A

carbamoyl phosphatase

60
Q

Where in the cell is carbamoyl phosphatease active?

A

the mitochondrial matrix

61
Q

What two places in a cell does the urea cycle take place?

A

the cytosol and mitochondrial matrix

62
Q

What can be considered the prep step of the urea cycle?

A

carbamoyl phosphtase

63
Q

Carbamoyl phosphate combines with L-ornithine to create?

A

L-citrulline

64
Q

What enzyme catalyzes the reaction that creates L-citrulline?

A

ornithine transcarbamoylase

65
Q

What compound adds the second NH3 in the urea cycle?

A

aspartate

66
Q

Aspartate combines with citrulline to create?

A

Argininosuccinate

67
Q

What enzyme catalyes the formation of argininosuccinate?

A

argininosuccinate synthase

68
Q

What enzyme catalyes the creating of arginine?

A

argininosuccinate lyase

69
Q

A by product of the creation of arginine is?

A

fumarate

70
Q

What enzyme cleaves off two amino groups to create urea?

A

arginase

71
Q

What enzyme catalyes the formation of ornithine?

A

arginase

72
Q

What is the compound that is the precursor for both amino groups donated to make urea?

A

glutamate

73
Q

Once glutamate dontes an amino group to oxaloacetate, what is formed?

A

aspartate

74
Q

If there is a low energy charge in the cell, what happens to an amino acid?

A

its oxidized to make ATP

75
Q

If blood glucose is low, what happens to an amino acid?

A

it is converted to enter gluconeogenesis to make glucose

76
Q

If there is a high enery charge and lots of glucose, what happens to an amino acid?

A

it is converted in to liver to be used in fat synthesis

77
Q

What are the 6 amino acids that skeletal muscle can metabolize?

A

LIVGAA

78
Q

During carbohydrate, fat, and protein burning, what are amino acids shipped to the liver on what compound?

A

alanine

79
Q

Alpha-ketoglutarate entering krebs cycle can be called what process?

A

anaplerosis

80
Q

What does anaplerosis mean?

A

Adding substrates from another metabolic process

81
Q

During exercise, having glycolysis run faster does what for amino acid metabolism?

A

to make extra pyruvate for picking up amino acids being oxidized in muscle

82
Q

An increase in pyruvate in the muscle during exercise aslo creates an increase in what else?

A

alanine to get nitrogen to the liver

83
Q

Glutamate concentrations in the plasma during exercise tend to?

A

decrease

84
Q

Alanine concentrations in the plasama during exercise tend to what?

A

increase

85
Q

SInce the muscle soaks up most BCAA’s and glutamate after a meal, how does the gut get AA?

A

the muscle exports glutamine to feed the areas that need it

86
Q

What are the 3 BCAA used by muscle?

A

Leucine, Isoleucine, and Valine

87
Q

What is over 90% of muscle amino acid uptake?

A

LIV and glutamate

88
Q

Muscle amino acid is released in lower amounts because?

A

its being used

89
Q

What are the most abundatly released amino acids?

A

Glutamine and alanine

90
Q

Glutamine and alanine are considered to be transporters, true or flase?

A

true

91
Q

List some conditions that would stimulate GNG from AA

A

low carbs, exercise, fasting, etc

92
Q

What are the only ketogenic AA’s?

A

leucine and lysine

93
Q

Describe how an AA can be made into fat?

A

AA to alpha-ketoacid into Acetyl-CoA then fatty acid

Biochemistry II (12 decks)

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