Amino Acid Synthesis and Degradation Flashcards

1
Q

What are sources of amino acids?

A

proteins, body proteins or one you eat. excess nitrogens.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the essential amino acids

A

PVT TIM HALL

phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, histidine, arginine, leucine, lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

essential vs. nonessential

A

essential - must eat in diet

nonessential - body can make from another source

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

3 phosphoserine to serine

A

phosphoserine phosphatase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

3 phoshphydroxy pyruvate to 3 phosphoserine

A

transamination and PLP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

3 phosphoglycerate into 3 phosphoydroxy pyruvate

A

3 phosphopyruvate dehydrogenase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Describe formation of serine

A

starting with 3phosphoglycerate (intermediate of glycolysis)

1) 3 phosphoglycerate via 3 phosphopyruvate dehydrogenase (using NAD+/NADH) becomes 3 phosphohydroxy pyruvate

2) 3 phospho hydroxy pyruvate via transamination reaction and PLP becomes 3 phoshposerine

2) 3 phosphoserine via phosphoserine phosphatase becomes serine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What intermediate of glycolysis is a precursor of serine?

A

3 phosphoglycerate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What starting material makes serine?

A

glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

formation of glycine

A

starts with serine; hydroxymethyl transferase and PLP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

serine hydroxymethyltransferase

A

main way for producing tetrahydrofolate derivatives. requires PLP as a cofactor.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

describe body catabolism of methionine

A

methionine becomes homocyteine via the methylation cycle. SAM gives a methyl group and S- adenosyl methionine becomes homocysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Draw homocysteine

A

1 carbon longer than cysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

describe synthesis of cysteine from serine and methionine

A

using the sulfur of methionine to become sulfur of cysteine. the rest of cysteine (carbons and nitrogen) comes from serine.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Where does the sulfur come from in cysteine?

A

it comes from methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Where do the nitrogens of cysteine come from

A

they come from serine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Cystathionine-β-synthase

A

homocysteine reacts with serine makes cystatione. PLP is required to make cysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Cystathionase

A

PLP required. Cystathione breaks apart. one is cysteine and one part is alpha ketobutyrate. Loss of nitrogen.. comes off as an ammonium.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

propionyl CoA carboxylase

A

proprionyl Coa (3 carbons) becomes methyl malonyl (4 carbons) Biotin, CO2, and ATP required.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

methylmalonyl coA mutase

A

requires vitamin B12 as a cofactor

methylmalonyl becoming succinyl CoA

propionyl becomes methyl malonyl

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what cofactor is required by methylmalonyl CoA mustase

A

vitamin B12

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

which amino acids lead to propionyl group?

A

VITM

valine, isoluecine, threonine, and methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

formation of alanine?

A

alanine transaminase (ALT), which converts L-glutamate and pyruvate into α-ketoglutarate and L-alanine. requires PLP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

formation of aspartate

A

oxaloacetate to aspartate via aspartate transamination and PLP

25
Q

formation of arginine

A

from aspartate; arginine synthetase; comes from glutamine side chain

26
Q

pyruvate carboxylase

A

pyruvate into oxaloacetate

27
Q

sources of propionyl CoA

A
  • cholesterol is turned into an unconjugated bile salt
  • priopionic acid made in the colon
  • fatty acid oxidation
28
Q

describe synthesis of glutamate from glucose and

A

glucose to pyruvate (via glycolysis)

pyruvate becomes acetyl coA via pyruvate dehydrogenase
pyruvate becomes oxaloacetate via the pyruvate carboxylase reaction

oxaloacetate and acetyl coA via citrate synthase go into TCA cycle

alpha ketoglutarate to glutamate via glutamate dehydrogenase.

ammonium ion added via glutamine synthetase reaction and this can be made glutamine

29
Q

2 amino acids made from glutamate

A

proline and arginine (via glutamate semialdehyde (arginine / ornithine/urea cycle)

30
Q

aromatic amino acids

A

tyrosine, tryptophan, phenylalanine

31
Q

how to synthesize tyrosine from phenyl alanine

A

hydroxylation reaction.

BH4 tetrahydrobioterin is required as second reducing agent (first reducing agent is phenylalanine) and the oxidizing agent is O2

32
Q

what is the biological cause of PKU disease? phenylketonuria

A

genetic mutation, can’t turn phenylalanine into tyrosine. phenylalanine builds to a dangerous level.

aspartame contains it.

classical = genetic mutation of phenylalanine hydroxylase

nonclassical - dihydrobioterine reductase mutation, doesn’t have enough BH4 to hydroxylate aromatic amino acids

33
Q

Six entry points for mainstream metabolism

A

pyruvate,

acetyl CoA

alpha ketoglutarate
succinyl coA (VITM) 

fumarate

oxaloacetate

34
Q

branched chain amino acids and their degredation

A

liver caells cannot break down but muscle cells can

transamination reactions

35
Q

why does the liver not break down branched chain amino acids?

A

branched chain aminoacid transaminase - mmuscle cells have lots of this and liver does not

36
Q

branched chain ketoacid dehydrogenase complex BCKADH

A

an alphaketoacid gets oxidized, decarboxylated and attached to coenzyme A

needs thiamine pyrophosphate, lipoic acid, and FAD.

37
Q

three enzymes that require lipoic acid as a cofactor

A

alpha ketoglutarate dehydrogenase
pyruvate dehydrogenase
branched chain ketoacid dehydrogenase

38
Q

enzymes with thiamine pyrophosphate in active site

A

alpha ketoglutarate dehydrognase
pyruvate dehydrogenase
branched chain ketoacid dehydrogenase
transketolase

39
Q

amino acid precursor for carnitine

A

lysine and methionine in the form of SAM

40
Q

glutathione perioxidase requires which cofactor

A

selenium

41
Q

amino acid precursor for glutathione

A

glutamate, cysteine, and glycine

42
Q

conjugation of bile salts

A

taurine and glycine

43
Q

amino acid required for synthesis of taurine

A

sulfur containing cysteine amino acid

44
Q

NAD nicotinamide adenine dinucleotide made from

A

tryptophan

45
Q

Tri-iodotyronine

A

T3

46
Q

Tetra-iodotyronine

A

T4

47
Q

thyroid hormones

A

tyrosine

48
Q

heme

A

glycine and succinyl coA is the intermediate

49
Q

creatine amino acid precursor

A

glycine and arginine and methionine

50
Q

epinephrine

A

requires methionine SAM

51
Q

melanins

A

tyrosine

52
Q

serotonin

A

tryptophan

53
Q

melatonin

A

tryptophan and methionine SAM

54
Q

Succinyl coA sources

A

VITM valine, isoleucine, threonine, methionine

55
Q

histamine

A

histidine

56
Q

gamma amino butyric acid

A

glutamate

57
Q

nitric oxide

A

arginine

58
Q

purine nucleotides

A

glutamine, glycine, aspartate

59
Q

pyrimidine nucleotides

A

glutamine and aspartate