BCH 202 Protein metabolism Flashcards

1
Q

Describe absorptionof amino acids

A

Free Amino Acids
O Absorption is carried out by Na+-dependent
amino acid cotransport in the luminal
membrane via facilitated diffusion.
O It is analogous to the cotransporter for
glucose and galactose.
O There are four separate carriers for neutral,
acidic, basic, and imino amino acids,
respectively.

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2
Q

Describe absorption of peptides

A

Peptides
O Dipeptides and tripeptides are absorbed by
H+-dependent cotransport in the luminal
membrane.
O Absorption of these peptides occur faster
than free amino acids.
O Cytoplasmic peptidases hydrolyze them to
amino acids which are then transported
from cell to blood by facilitated diffusion.

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3
Q

Clinical correlation of protein absorption

A

Neutral Amino Aciduria (Hartnup Disease)
O Mutation in the epithelial transport of
neutral amino acid.
O Characterized by the inability of renal and
intestinal epithelial cells to absorb neutral
amino acids from the lumen.
This results in malabsorption of free amino acids from the diet.

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4
Q

Site of amino acids catabolism

A

O The principal site of amino acid metabolism
is the Liver
O However, this occurs in other tissues such
as the kidney, muscle, adipose tissue, and
small intestine.

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5
Q

Stages of amino acid catabolism

A

O Transamination
O Oxidative deamination

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6
Q

All amino acids undergo
transamination reaction except
which 3?

A

lysine, proline, and threonine

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7
Q

What happens to the ammonium ion formed?

A

The Ammonium ion formed is converted to Urea, excreted in the urine……..Urea cycle

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8
Q

Describe nitrogen excretion

A

O Nitrogen is removed via urea cycle.
O 2 sources are ammonia and aspartate.
O 4 ATPS are required for this cycle.
O SLC25A15, a transporter for citrulline

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9
Q

Clinical correlates of protein catabolism

A

Hyperammonemia
O Occurs when nitrogen excretion is impaired
due to liver failure or inborn error of
metabolism.
O Ammonia crosses the blood brain barrier,
enters the brain, depletes the brain of alpha
ketoglutarate (what then happens???)
O Can be managed by the use of antibiotics
O Lactulose

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10
Q

How is protein catabolism regulated?

A

REGULATION
O Allosterism: Glutamate dehydrogenase is regulated
allosterically by purine nucleotides
O GTP and ATP are allosteric activators in the
direction of glutamate synthesis
O Enzyme Induction

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