Amino Acid Metabolism - Catabolism Flashcards

1
Q

How do the different enzymes of the small intestine function?

A

Enteropeptidase -> Cleaves trypsinogen
Aminopeptidase -> Exopeptidases which chew from N-terminus
Dipeptidase -> Brak apart dipeptides

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2
Q

What determines the rate of ubiquitination of proteins destined for the proteosome?

A

Identity of the terminal N Amino Acids

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3
Q

What are the possible outcomes of ubiquitination?

A
  • Degradation
  • Recycling
  • Factor recruitment
  • Change of localization or activity
  • Disruption of interactions
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4
Q

What is the general structure of the Proteosome?

A
  • ATPase
  • 20S Catalytic domain
  • 19S regulatory domain
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5
Q

What can happen to amino acids after being degraded by the proteosome?

A
  • Dispose of Nitrogen via Urea Cycle
  • Make a new protein
  • Repurpose Carbon Skeleton
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6
Q

What is the process of deamination of amino acids?

A

Most follow 2 step Enzymatic reaction:

  • Aminotransferase
  • Glutamare dehydrogenase
  • Pyridoxal phophate is coenzyme

** Exception is Serine and Threonine which use Dehydratase

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7
Q

What is the role of ALT/SGPT?

A

Catalyzes interconversion of Alanine/Pyruvate

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8
Q

What is the role of AST/SGOT?

A
  • Catalyzes interconvention of Aspartate and Oxaloacetate
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9
Q

What is the substrate/process used to transport NH4+ from most tissues to the Liver?

A

Glutamate + NH4+ –> Glutamine —-> Glutamate + NH4+ (in Liver)

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10
Q

How is NH4+ transported from muscle tissue to the liver?

A

NH4+ –> Glutamate -> Pyruvate –> Alanine -> Glu (In liver) -> NH4+ (In liver)

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11
Q

Describe the first step of the Urea Cycle.

A

Carbomoyl phosphate Synthetase I (CSPI) combines CO2 (from TCA) and NH3 to make Carbamoyl Phosphate using 2 ATP.

*Comited step

**NAG is an allosteric activator

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12
Q

Describe the second step of the Urea cycle.

A

Ornithine is transprted ino mt to combine with Carbamoyl Phosphate to form Citrulline. Citrulline is exported to the cytoplasm.

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13
Q

Describe step 3 of the urea cycle.

A

Aspartate donates an NH3 to citralline to form arginine and fumarate.

*Uses 2 ATP

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14
Q

Describe the last step of the Urea cycle.

A

Addition of water cuases release of urea from Arginine. Ornithine is regenerated.

*Fumarate created in last step regenerated to OAA using TCA.

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15
Q

What are the different fates of protein carbon skeletons?

A

Glucogenic -> Gluconeogenesis

Ketogenic -> Ketone Bodies

Both Glucogenic and Ketogenic

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16
Q

What Carbon skeletons can be converted to OAA?

A
  • Asparagine

- Aspartate: Exchanged via SGOT

17
Q

What Carbon Skeletons are converted to a-Ketoglutarate?

A
  • Gluamine:Deamination to glutamate
  • Pro,Arg, His
  • Glutamate: Glutamate dehydrogenase
18
Q

What carbon skeletons are converted to Succinyl CoA?

A

Met, Val, Ile

19
Q

What Carbon skeletons can be converted to pyruvate?

A
  • Serine
  • Threonine
  • Glycine: Converted to Serine
  • Alanine: Exchanged by SGPT
  • Cystein: must also be desulfonated
20
Q

What amino acids are only Ketogenic?

A

Leucine and Lysine

21
Q

What amino acids are Glucogenic and Ketogenic?

A
  • Isoleucine
  • Phenylalanine
  • Threonine
  • Tryptophan
  • Tyrosine
22
Q

What amino acids are only glucogenic?

A
  • Alanine
  • Arginine
  • Asparagine
  • Aspartate
  • Cysteine
  • Glycine
  • Glutamate
  • Glutamine
  • Histidine
  • Methionine
  • Serine
  • Tryptophan
  • Valine