Block 2 Lecture 4 -- Amino Acid Synthesis Flashcards

1
Q

What are the essential amino acids?

A

1) Phe
2) Val
3) Thr
4) Try
5) Ile
6) Met
7) His
8) Arg
9) Leu
10) Lys

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2
Q

Which amino acids are synthesized from glycolysis intermediates?

A

1) Ser
2) Gly
3) Cys
4) Ala

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3
Q

What amino acids are synthesized from TCA intermediates?

A

1) Arg
2) Asp
3) Asn
4) Glu
5) Gln
6) Pro

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4
Q

What amino acids do not have transamination pairs?

A

1) Lys
2) Pro
3) Thr

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5
Q

Which non-essential amino acid is not derived from glycolysis/TCA?

A

Tyr (from the essential Phe)

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6
Q

What is the TA pair for Glu?

A

a-KG

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7
Q

What is the TA pair for Asp?

A

OAA

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8
Q

What is the TA pair for Ala?

A

Pyruvate

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9
Q

What is the TA pair for Gly?

A

glyoxylate

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10
Q

What is the TA pair for ornithine?

A

Glu-5-Semialdehyde

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11
Q

How can serine be synthesized?

A

1) 3-phosphoserine phosphatase – from 3-PG, direct product of glucose via 3-PGDH
2) serine hydroxymethyltransferase – from glycine (THF)

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12
Q

What compounds can serine synthesize?

A

1) serine dehydratase = pyruvate
2) + homocysteine –> cystathionine –> cysteine
3) serine hydroxymethyltransferase = glycine via THF

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13
Q

how is serine synthesis induced?

A

1) 3-PGDH induction

2) release of phosphoserine phosophatase feedback inhibition

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14
Q

How is glycine synthesized?

A

1) Serine hydroxymethyltransferase

2) Thr aldolase

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15
Q

How is glycine degraded?

A

1) GCC donates carbon to FH4, produces CO2 + NH4
2) D-amino-oxidase oxidizes to glyoxylate
3) TA to glyoxylate with Ala/pyruvate

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16
Q

What is the cofactor in GCC?

A

NAD & FH4

17
Q

What is the cofactor in Thr aldolase?

A

PLP

18
Q

How is cysteine synthesized?

A

1) cystathionine synthase then cystathionase

19
Q

What reactions does cysteine do?

A

1) desulfhydrase
- - donates NH3 to Glu
- - carbons become pyruvate
- - sulfate to urine

20
Q

What is the cofactor in cystathionine synthase?

A

PLP

21
Q

What reaction does cystathionine synthase catalyze?

A

Ser + Homocysteine –> Cystathionine

22
Q

What is the cofactor in the cystathionase reaction?

A

PLP

23
Q

What reaction does cystathionase catalyze?

A

Cystathionine + H2O –> a-KB + cysteine + NH4

24
Q

How is alanine produced?

A

transamination with pyruvate – especially in muscle

25
Q

How is Glu produced?

A

1) TA with a-KG
2) from Gln (Glutaminase)
3) from FIGLU (His & THF)

26
Q

What reactions does Glu take part in?

A

1) Gln synthase
2) TA
3) Glu DH (urea cycle)
4) reductase & phosphorylation –> Glu-5-SA

27
Q

How is Pro synthesized?

A

1) spontaneous cyclization of G5SA

2) reduction (FAD/NAD)

28
Q

What is the co-factor in GluDH?

A

NAD

29
Q

How is glyoxylate degraded?

A

1) oxidized to oxalate
…or….
2) to a-KG with TPP as cofactor

30
Q

What functional group is produced when G5SA cyclizes?

A

Schiff base/imine

31
Q

Where does proline synthesis occur in the cell?

A

1) Glu phosphorylation –> G5SA in mitochondria

2) G5SA reduced to Pro in cytosol

32
Q

How is arginine produced?

A

1) G5SH TA to ornithine, enters urea cycle

2) Arginase produces Arg

33
Q

Where does TA occur with G5SH?

A
  • *on the side chain

- - an oddity

34
Q

What happens when ornithine is in excess?

A

G5SA increases

Glu increases

35
Q

What amino acids are synthesized form G5SA

A

Proline & Arginine

36
Q

What is a sign of folate deficiency related to His metabolism?

A

FIGLU would be found in urine

37
Q

How is aspartate synthesized?

A

1) TA with OAA (PLP)

2) Asn-ase (hydrolytic non-oxidative deamination)

38
Q

How is Asn synthesized?

A

1) Asn synthetase (requires ATP & Gln)

39
Q

What cofactors does Asn synthetase require?

A

1) ATP

2) Gln –> Glu