PROTEIN METABOLISM I Flashcards

1
Q

continuous degradation and resynthesis of all cellular proteins

A

protein turnoever

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2
Q

susceptibility of a protein to degradation is expressed as its

A

HALF LIFE

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3
Q

half-lives for liver proteins range from under

A

30 mins to over 150 minutes

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4
Q

proteins with half lives over 100 hours include

ALC

A

aldolase, lactate dehydrogenase, and cytochromes

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5
Q

two major pathways that degrade intracellular proteins of eukaryotic cells

A

lysosomal degradation
ubuiquitin

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6
Q

lysosomes have a selective pathway which is activated only after a prolonged fast, that imports and degrades cytosolic proteins containing the pentapeptide KFER1 (lys-phe-glu-arg-gln) or a closely related sequence

A

Lysosomal degredation

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7
Q

proteins are marked for degradation by covalently linking them to ____________

A

ubiquitin

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8
Q

3 amino acids that are not metabolized in the liver

A

Valine Leucine Isoleucine

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9
Q

Valine Leucine Isoleucine are metabolized in the __________

A

brain and muscles

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10
Q

amino acids that can not be synthesized by the body so they must be provided in the diet

A

essential or indispensible amino acids

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11
Q

amino acids can be synthesized by the body so they need not be provided in the diet

A

non-essential or dispensible

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12
Q

semi-essential amino acid

A

arginine

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13
Q

3 enzymes that occupy central positions in amino acid biosynthesis

G-G-A

A

glutamate dehydrogenase
glutamine synthetase
aminotransferases

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14
Q

3 enzymes that occupy central positions in amino acid biosynthesis

used to synthesize glutamic acids

A

glutamate dehydrogenase

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15
Q

3 enzymes that occupy central positions in amino acid biosynthesis

used to synthesize glutamine

A

glutamine synthetase

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16
Q

3 enzymes that occupy central positions in amino acid biosynthesis

enzymes that are used for transamination
can be used to synthesize many other amino acids

A

aminotransferases

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17
Q

types of amino acid catabolism

Removal
D
O
O

A

removal of alpha-amino group
decarboxylation
oxygenation
one carbon transfer

18
Q

removal of alpha amino group

amino acid —-> keto acid + NH3

A

oxidative deamination

19
Q

glu is the only amino acid that

undergous oxidative deamination at an appreciable rate in mammalian tissues

A

glutamate dehydrogenase

20
Q

the most active amino group acceptor

A

alpha ketoglutarate

21
Q

remember that in your amino acids are ________ acids

A

L-Amino Acids

22
Q

abnormal neural development generalized aminoaciduria absence of peroxisomes in a liver biopsy

aminoaciduria is due to deficient amino acid oxidase activity

L amino acid oxidase activity

A

zellweger cerebrohepatorenal syndrome

23
Q

non-oxidative deamination

requires pyrodoxal phosphate (B6PO4) as cofactor

hydroxy amino acids (serine, threonine, tyrosine, homoserine)

A

amino acid dehydrases

24
Q

non-oxidative deamination

requires pyrodoxal phosphate (B6PO4) as cofactor

sulfur containing amino acids (cysteine, homocysteine, methionine)

A

amino acid desulfydrases

25
Q

_________- produces a new keto acid and a new amino acid

enzyme: transaminase/aminotransferase

A

transamination

26
Q

leads to formation of biogenic amines

A

decarboxylation

27
Q

examples of decarboxylation are

S
H
C

A

serotonin
histamine
catecholamines

28
Q

ways of detoxifying ammonia are

Reversal
G formation
U formation
A formation

A

glutamate dehydrogenase
glutamine formation
urea formation
asparagine formation

29
Q

glutamine formation

whenever ammonia reaches the brain, the brain combines it with glutamic acid , converting it to glutamine using the enzyme _______

A

glutamine synthetase

30
Q

major source of ammonia excreted in the urine?

A

glutamine

31
Q

most nitrogenous excretory product

serves as the disposal form of ammonia, toxic particularly to the brain and CNS

A

urea

32
Q

how many ammonias are detoxified in the urea cycle

A

2 amonnias

33
Q

how many ATPs are priduced in the Urea cycle pathway?

A

4 ATPs

34
Q

major control points of urea pathway

CPS
OT
A

A

carbamoyl phosphate synthetase I
ornithine transcarbamoylase
Arginase

35
Q

HHH syndrome

due to the mutation of the ornithine transporter gene (ORNT1)

3 manifestations are

A

hyperammonemia
hyperornithinemia
homocitrullinuria

36
Q

in the 4th reaction, Argininosuccinate is cleaved to form fumarate and _______

A

arginine

37
Q

enzyme deficient in hyperammonemia type 1

A

carbamoyl phosphate synthetase I

38
Q

enzyme deficient in hyperammonemia type 2

A

ornithine transcarbamoylase

39
Q

enzyme deficient in citrullinemia

A

argininosuccinate synthetase

40
Q

enzyme deficient in argininosuccinate aciduria

A

argininosuccinase

41
Q

enzyme deficient in arginemia

A

arginase