Amino acid Metabolism Flashcards

1
Q

Amino acids for energy

A
  1. Normal protein turnover
    - catabolized to energy of not required for synthesis of proteins
  2. High protein diet
    - excess amino acids
    - can not be stored
  3. Starvation
    - no carbohydrates, fats
    - body catabolizes cellular protein, mostly from muscle
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2
Q

Location of dietary protein breakdown

A

mainly in liver

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3
Q

Dietary protein to stomach

A

stimulate G cells to secrete gastrin

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4
Q

Role of gastrin

A

stimulates chief cells- pepsinogen

parietal cells - HCL

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5
Q

Role of HCl in breakdown

A

kill bacteria/foreign particles
denature dietary proteins
stimulate pepsinogen - pepsin

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6
Q

Role of pepsin

A

catalyses the breakdown of polypeptide to many smaller pieces

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7
Q

Peptides to duodenum

A

stimulate duodenum - secretin + CCK

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8
Q

Role of secretin

A

stimulate release of HCO3- from pancreas - pH to normal

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9
Q

Role of CCK

A

stimulates exocrie pancreas to release zymogens:
trypsinogen - ENETROPEPTIDASE - trypsin
chymotrypsinogen - TRYPSIN - chymotrypsin
proelastase - TRYPSIN - elastase
procarboxypeptidases - TRYPSIN - carboxypeptidase

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10
Q

Role of proteases

A

cleave peptides smaller

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11
Q

Role of peptidases

A

Carboxypeptidase - remove COO- terminal AAs

Aminopeptidase - remove NH2 terminal AAs

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12
Q

Transport of AAs

A

gluthatione ( gamma-glutamyl cycle)

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13
Q

Protein turnover

A

external: collagenases, metalloproteases, elastases
internal: catepsins, ubiquination

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14
Q

Transamination reaction

A

alpha-AA + alpha-ketogluatarate -> alpha-ketoacid + glutamate

enzyme: Aminotransferase
coenzyme: PLP

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15
Q

Pyridoxal phosphate PLP

A

from vitamin B6
cofactor in all reactions concerning aminotransferases
bound to Lys residue of enzyme as Schiff base
grabs NH4+ from AA and gives it to KG
PLP -> pyridoxamine phosphate -> PLP

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16
Q

ALAT and ASAT

A

ALAT (alanine aminotransferase): in liver
ASAT(aspartate aminotransferase): heart/muscle
non-functional plasma enzymes
markers of tissue damage

17
Q

Glutamate Dehydrogenase

A

Glu + H2O + NAD+ -> alpha-KG + NH4 + NADH
NH4 goes to urea cycle
alpha-KG to TCA

18
Q

Allosteric regulation of Glutamate DH

A

activated by ADP

inhibited by GTP

19
Q

Isoenzymes of Glutamate DH

A

GLUD1: liver, kidney etc.
GLUD2: brain, testis

20
Q

Glutamine synthase

A

in extrahepatic tissue
NH4 attached to Glu -> Gln
transported to liver, kidney

21
Q

Glu -> Gln

A

Glu + ATP -> gamma-glutamyl P + ADP.. +NH3 -> Gln + Pi

enzyme: glutamine synthase

22
Q

Glutaminase

A

in liver mitochondria
Gln -> Glu
+H20
-NH4 (to urea cycle)

23
Q

Glucose- Alanine cycle

A

glucose - pyruvate - alanine - pyruvate -glucose
enzyme: alanine aminotransferase ALAT
NH4+ from muscle transported to liver

24
Q

Deamination

A
  1. Oxidative deamination
    - Glu DH
  2. Catabolism
    - Ser (Thr) dehydratase
    - His + Gly
  3. Flavoproteins
    - L-AA oxidase
    - D-AA oxidase
  4. Loss of beta/gamma amide
    - glutaminase
    - asparginase
  5. Nucleotide metabolism
25
Q

Incorporation of free ammonia

A
  1. Glu DH - at high ammonia conc.
  2. Carbamyl-P synthetase- urea cycle
  3. Gln synthetase