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?

17
Q

What is the cofactor in Thr aldolase?

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?

21
Q

What reaction does cystathionine synthase catalyze?

A

Ser + Homocysteine –> Cystathionine

22
Q

What is the cofactor in the cystathionase reaction?

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
How is Glu produced?
1) TA with a-KG 2) from Gln (Glutaminase) 3) from FIGLU (His & THF)
26
What reactions does Glu take part in?
1) Gln synthase 2) TA 3) Glu DH (urea cycle) 4) reductase & phosphorylation --> Glu-5-SA
27
How is Pro synthesized?
1) spontaneous cyclization of G5SA | 2) reduction (FAD/NAD)
28
What is the co-factor in GluDH?
NAD
29
How is glyoxylate degraded?
1) oxidized to oxalate ...or.... 2) to a-KG with TPP as cofactor
30
What functional group is produced when G5SA cyclizes?
Schiff base/imine
31
Where does proline synthesis occur in the cell?
1) Glu phosphorylation --> G5SA in mitochondria | 2) G5SA reduced to Pro in cytosol
32
How is arginine produced?
1) G5SH TA to ornithine, enters urea cycle | 2) Arginase produces Arg
33
Where does TA occur with G5SH?
* *on the side chain | - - an oddity
34
What happens when ornithine is in excess?
G5SA increases | Glu increases
35
What amino acids are synthesized form G5SA
Proline & Arginine
36
What is a sign of folate deficiency related to His metabolism?
FIGLU would be found in urine
37
How is aspartate synthesized?
1) TA with OAA (PLP) | 2) Asn-ase (hydrolytic non-oxidative deamination)
38
How is Asn synthesized?
1) Asn synthetase (requires ATP & Gln)
39
What cofactors does Asn synthetase require?
1) ATP | 2) Gln --> Glu