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Block 3 Week 6 > TBL Amino Acid Metabolism > Flashcards

TBL Amino Acid Metabolism Flashcards

1
Q

This is made in bacteria, it is the reduced form of folate and transfers single carbons

A

THF

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2
Q

This made from ATP and methionine and transfers methyl groups and makes SAhcys and hcys

A

SAM

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3
Q

This transfers CO2.

A

biotin

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4
Q

This is involved in oxidation reactions (tyrosine synthesis)

A

tetrahydrobiopterin

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5
Q

This holds nitrogen and is the coenzyme form of B6 and cofactor for tranaminase reaction.

A

PLP (pyridoxal phosphate)

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6
Q

Why do we need A.As?

A

energy source
substrate for proteins
substrate for heme, purine, pyrimidines, melanine

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7
Q

What part of the TCA cycle inhibits glycolysis?

A

citrate

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8
Q

Whenever you see the word dehydrogenase with the word of the substrate in it what do you make?
If you see dehydrogenase with the word of the product in it what does it make?

A

NADH
(except with succinate dehydrogenase you make FADH2)
NAD+ or NADP+

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9
Q

How much energy do you get from TCA cycle?

A

12 ATP

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10
Q

What can malate turn into?

A

oxaloaceteate

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11
Q

What is the breakdown of alcohol?

A

alcohol->ADH acetalaldehyde-> acDH acetic acid-> acetyl coA

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12
Q

In the TCA cycle when you see a synthetase what do you get?

A

ATP

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13
Q

What is made in the liver and is driven by too much ammonia?

A

glutamate synthesis

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14
Q

If you see an enzyme with synthetase or dehydrogenase with the word of the substrate in it (i.e succinyl coa -> succinate; uses succinyl CoA synthetase) then do you gain or lose energy?

A

you gain energy

you will use energy if the enzyme has the name of the product i.e glutamate-> glutamine using glutamine synthase

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15
Q

Why would you want to turn glutamate into glutamine?

A

because glutamate doesnt transport across cell membranes and glutamine does

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16
Q

What is the most abundant amino acid and it allows the movement of untoxic NH4 and donates nitrogens?

A

glutamine

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17
Q

Are transaminases reversible and what do they require?

A

yes!

PLP (B6)

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18
Q

What are serum ALT used for?

A

as a liver diagnositic test

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19
Q

What is a side product of the creation of glutamine back to glutamate and what do we do with it?

A

NH4+

goes to urea cycle

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20
Q

Where is the glucose-alanine cycle?

A

in the muscle and the liver

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21
Q

What does cortisol do?

A

it stimulates alanine aminotransferase and gluconeogenesis and breakdown of proteins in the muscle

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22
Q

Where does the glucose-glutamine cycle take place?

A

in the kidney and the muscle

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23
Q

What A.A is often glycosylated?

A

ASN

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24
Q

DO humans express asparaginase?

A

no

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25
Q

What does leukemia do to ASN?

A

makes body unable to make it so you will need ASN injections

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26
Q

What is the vehicle for transferring carbons of intermediate oxidation states?

A

serine hydroxymethyltransferase

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27
Q

When 3PGA goes to Ser there are 2 types of intermediates, what are they?

A

phosphopyruvate and phosphoserine intermediates

this generates NADH

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28
Q

Deficiencies in what 2 enzymes cause homocystinuria, characterized by a mentally deficient gumbee like body with fragile bones and blood clots.
How do you treat this?

A

cystathionine synthase (need PLP)
cystathionase (PLP)
Cuz Sisters need PeePs

Good diet and vitamins

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29
Q

If you have an enzyme defiency resulting in PKU, what enzyme are you deficient in?

A

phenylalanine hydroxylase

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30
Q

What are the symptoms of PKU and how do you treat it?

A

light skin, mental retardation

no aspartame, diet

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31
Q

Where do you begin digesting proteins and how?

A

stomach via low pH, gastrin from mucosa triggers pepsin, parietal cells (HCl) and renin (coagulates milk)

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32
Q

What happens to proteins in the intestine?

A

Low ph->bicarb from pancreas

CCK release-> triggers pancreatic enzymes

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33
Q

What activates trypsin and where does it come from?

A

enteropeptidase from the intestine

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34
Q

Explain ubiquitin

A

attaches to lysine to degrade proteins
the longer the chain the stronger the degredation signal
N terminal determines speed of degredation
-arginine and leucine-> fast
-methionine and proline-> slow

35
Q

What are PEST sequences?

A

Pro-Glu-Ser-Thr; this sequence is a target for degredation

36
Q

What digests ubiquitin-tagged proteins?

A

proteosomes

37
Q

What are diseases associated with ubiquitones?

A

Alzheimers and Parkinsons
Cystic fibrosis
Liddle’s syndrome

38
Q

(blank) diseases are associated with the formation of proteins structures in neurons

A

alzeheimers and parkinsons

39
Q

(blank) disease is the rapid degradation of chloride channels

A

cystic fibrosis

40
Q

(blank) is when Na+ channels in kidney dont get degraded and you get excessive Na absorption and early onset hypertension

A

Liddles

41
Q

Who have positive nitrogen balance?

A

children, pregnant women and body builders

42
Q

What give negative nitrogen balance?

A

stress hormones, cytokines

43
Q

What are ketogenic amino acids?

A

ones that make Acetoacetyl Coa, Acetyl Coa

the A’s :)

44
Q

What are glucogenic amino acids?

A

ones that make pyruvate, oxaloacetate, fumarate, succinyl coA, alpha ketoglutarate

45
Q

If there is a defect in glycine transaminase what does this lead to?

A

oxaluria Type I

Too much oxalate (makes kidney stones)

46
Q

If there is a defect in glycine cleavage enzyme that what does this lead to?

A

nonketotic hyperglycinemia (too much glycine)

47
Q

If you have a defect in cystathionine synthase what does this lead to?

A

homocystinuria

cant make amino acids

48
Q

What amino acids degrade to pyruvate?

Slide 25

A

Some Good Children Are Toothless Mean Pirates

Serine, Glycine, Cysteine, Alanine, Tryptophan, methionine, Pyruvate

49
Q

What amino acids degrade to acetyl Coa?

A

Prostitutes Like Taking In Long Things

Phenylalanine, Leucine, Tyrosine, Isoleucine, Lysine, Tryptophan

50
Q

If you have a deficiency in tyrosine aminotransferase what will you have?

A

tyrosinemia II (too much tyrosine)

51
Q

If you have a deficiency in homogenitisate oxidase then what will you have?

A

homogentisic acid intermed. alkaptonuria

52
Q

If you have a deficiency in fumarylacetoacetate hydroxylase then what will happen?

A

fumarylacetoacetate intermediate tyrosinemia I

53
Q

What amino acids degrade to alpha ketoglutarate?

A

Gregs Hot Girlfriends Are Pregnant

Glutamate, Histidine, Glutamine, Arginine, Proline

54
Q

If you have a deficiency in histidase then what will you have?

A

histidinemmia

55
Q

If you have folate deficiency what will accumulate?

A

formimino glutamic acid

FIGLU

56
Q

What amino acids degrade to OAA?

A

ASS
Asparagine
Asparatate

57
Q

Simplify branched chain amino acid degredation

A

transamination in MUSCLE followed by oxidative decarboxylation in LIVER

58
Q

What happens if you lack alpha keto acid dehydrogenase complex?

A

maple syrup urine disease

59
Q

What are the products of branched chain amino acid metabolism?

A

proprionyl CoA
Acetyl CoA
Acetoacetate

60
Q

What amino acids degrade to succinyl CoA?

A

I Think My Vagina Sux

Isoleucine, Threonine, Methionine, Valine, Succinyl CoA

61
Q

If you have a deficiency in methylmalonyl CoA mutase what will result?

A

methylmalonic aciduria

62
Q

Where are glutamine and glutamate metabolized?

A

the intestinal mucosa

63
Q

Where are amino acids other than glutamine and glutamate metabolized?

A

the liver

64
Q

Where do branched chain amino acids go to get metabolizd?

A

Start in liver and go to muscle and then go back to liver

65
Q

What is the major source of amino acids during fasting?

A

muscle

66
Q

During fasting,Where does alanine go for gluconeogenesis?

A

liver

67
Q

During fasting where does glutamine go?

A

to the kidney and intestines

68
Q

In the phenylalanine amino acid degredation pathway, what are the 2 missing enzymes that can result in phenylalanine accumulate and PKU?

A

phenylalanine hydroxylase -> PKU classical
dihydropteridine reductase-> PKU nonclassical
Both result in mental retardation

69
Q

Tell me about homogentisate oxidase;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

tyrosin pathway
homogentisic acid accumulates
alcaptonuria
Black urine, arthritis

70
Q

Tell me about fumarylacetoacetate;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

tyrosine
fumarylacetoacetate
tyrosinemia I
liver failure, early death

71
Q

Tell me about tyrosine aminotransferase;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

tyrosine
tyrosine
tyrosinemia II
neurological defects

72
Q

Tell me about cystathionase;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

methionine
cystathionine
cystathionura
benign

73
Q

Tell me about cystathionine synthase;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

methionine
homocysteine
homocysteinuria
CV and neurological problems

74
Q

Tell me about glycine transaminase;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

glycine
glyoxylate
primary oxaluria Type I
Renal failure due to stone formation

75
Q

Tell me about glycine cleavage enzyme;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

glycine
glycine
hyper glycinemia
mental retardation

76
Q

Tell me about branched chain alpha keto acid dehydrogenase;

what AA pathway is it in, what accumulates, what is the disease associated with it and what are the symptoms?

A

branched chain amino acids (leucine, isoleucine, valine)
alpha ketoacids of the branched chain amino acids
maple syrup urine
mental retardation

77
Q

(blank) is a neurotoxin so must be converted to carbamoyl phosphate to enter the urea cycle.

A

ammonia (NH4+)

78
Q

Build up of what leads to orotate in the urine?

A

carbamoyl phosphate

79
Q

How do you measure Blood urea levels?

When are these levels high?

A

As BUN

Renal failure

80
Q

What enzyme can cleave urea to alkalize the urine and cause precipitation of magnesium ammonium phosphate (kidney stones)?

A

bacterial enzyme Urease

81
Q

What can inherited defects in the urea cycle cause?

A

hyperammonemia and encephalopaty
feeding difficulties, vomiting, lethargy, irritiability, aversion to protein rich foods
ATP deficiencies (Cuz alpha KG-> glutamine)
High glutamine levels

82
Q

How do you treat urea cycle enzyme deficiency?

A

limit protein intake
remove excess ammonia
replace intermediates missing from urea cycl
liver transplant

83
Q

Where does the urea cycle take place?

A

the liver

84
Q

How many ATPs are needed in the urea cycle and where do they come from?

A

4,
2 from carbamoyl synthetase
2 from argininosuccinate synthase

Block 3 Week 6 (6 decks)

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