Amino acid oxidation Flashcards

1
Q

amino acids to acetyl CoA

Keto genic

A
T I F K L W Y
Threonine 
Isoleucine 
Phenylalanine
Lysine 
Leucine
Tryptophan 
Tyrosine
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2
Q

amino acids to pyruvate

A
C A W G S T 
cysteine 
Alanine
tryptophan
glycine
serine
threonine
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3
Q

alpha ketoglutarate

A
R E H P Q
Arginine
Glutamate 
Histodine
Proline
Glutamine
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4
Q

succinyl- CoA

A
I M T V 
Isoleucine 
Methionine 
Threonine 
Valine
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5
Q

fumarate

A

F Y
Phenylalanine
Tyrosine

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6
Q

oxaloacetate

A

N D
Asparagine
Aspartate

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7
Q

Albinism

A

Melanin synthesis from Tyrosine

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8
Q

Alkaptonuria

A

Tyrosine degredation

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9
Q

Argininemia

A

Urea synthesis

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10
Q

Argininosuccinic acidemia

A

urea synthesis

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11
Q

Carbamoyl phosphate synthetase 1 deficiency

A

Urea synthesis

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12
Q

Homocystinuria

A

Methionine degradation

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13
Q

Maple syrup urine disease (branchedchain ketoaciduria)

A

Isoleucine, leucine and valine degradation

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14
Q

Methylmalonic acidemia

A

conversion of propionyl-CoA to succinyl-CoA

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15
Q

Phenylketonuria

A

conversion of phenylalanine to tyrosine

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16
Q

How does ubiquitin tag a protein?

A

Attached to the activating enzyme by hydrolyzing an ATP to AMP

ubiquitin is transferred to the conjugating enzyme

a ligase enzyme transfers the ubiquitin to the substrate

17
Q

how does the proteasome breakdown proteins

A

19S regulatory structure recognizes ubiquitinylated proteins to direct them into the 20S core

20S core has protease activity. Trypsin like
chymotrypsin like and peptidylglutamyl-peptide hydrolyzing

ATP is needed to take off the ubiquitin and breakdown the protein into amino acids