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Metab Lec

Amino acids undergo degradation through several stages: transamination, oxidative deamination, ammonia transport, and the urea cycle. Transamination involves transferring the amino group from an amino acid to an alpha-ketoglutarate, catalyzed by transaminase enzymes. This converts the amino acid to an alpha-keto acid and glutamate. Oxidative deamination then removes the amino group as ammonia. Ammonia is transported to the liver to enter the urea cycle, where it is synthesized into urea for excretion. The carbon skeletons of amino acids can be converted into intermediates for energy production or gluconeogenesis.

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55 views68 pages

Metab Lec

Amino acids undergo degradation through several stages: transamination, oxidative deamination, ammonia transport, and the urea cycle. Transamination involves transferring the amino group from an amino acid to an alpha-ketoglutarate, catalyzed by transaminase enzymes. This converts the amino acid to an alpha-keto acid and glutamate. Oxidative deamination then removes the amino group as ammonia. Ammonia is transported to the liver to enter the urea cycle, where it is synthesized into urea for excretion. The carbon skeletons of amino acids can be converted into intermediates for energy production or gluconeogenesis.

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lovelots1234
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AMINO ACID METABOLISM

Lourdes L. Balcueva, M.D.

OBJECTIVES
1.

To discuss different factors that affect


degradation of proteins
2. Discuss the stages by which the amino
acid nitrogen is catabolized and excreted:
a. transamination
b. oxidative deamination
c. ammonia transport
d. urea cycle

OBJECTIVES
5. Describe the conversion of the
carbon skeleton of each amino acid
to amphibolic intermediates.
6. Classify the different amino acids
into 3 groups:
a. glycogenic or glucogenic
b. ketogenic
c. both glucogenic and ketogenic

OBJECTIVES
7. Discuss the inborn errors
associated with the catabolism of
the carbon skeleton of amino acids
and the urea cycle.

Amino acids can undergo


oxidative degradation:
1. Normal synthesis and
degradation of cellular
proteins
2. In diet rich in protein in
excess of bodys needs for
protein
3. During starvation

daily protein degradation- 1-2


% of total body protein
-75% is reused for protein
synthesis
- half-life (t)- time required for
a protein molecule to degrade

- PEST (proline, glutamate,


serine, threonine)- proteins with
this sequence of amino acids
are rapidly degraded.

ATP independent lysosomal


degradation of protein:
1.

Extracellular
2. Membrane associated
3. Long-lived intracellular proteins
ATP dependent and Ubiquitin is required:
1. Abnormal proteins
2. Short-lived proteins
- degradation takes place in proteasome

Enzymes that degrade body


proteins:
1. Proteases- hydrolyze
internal peptide chains
2. Amino peptidases and
carboxy peptidases
3. Lysosomal proteases
(cathepsins)- degrades
asialoglycoproteins ex.

4 STAGES OF CATABOLISM
OF AMINO ACIDS
1. Transamination
2. Oxidative deamination
3. Ammonia transport
4. Reaction of the urea cycle

Transamination

Transamination

Transamination

TRANSAMINATION

B6 derivative present in
catalytic site of enzyme;

Serves as carrier of amino


acid

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