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PROTEIN METABOLISM

BY
DR UTPAL DONGRE
TRANSAMINATION
Transamination, a chemical reaction that
transfers an amino group to a ketoacid to
form new amino acids. This pathway is
responsible for the deamination of most
amino acids.
MECHANISM OF TRANSAMINATION
OXIDATIVE AND NON OXIDATIVE
DEAMINATION
Transport of ammonia

FIG: TRANSPORT OF AMMONIA BY GLUTAMINE


FIG: GLUCOSE ALANINE CYCLE
UREA CYCLE
1: Ornithine transcarbamylase. 2: Arginosuccinic synthetase. 3: Arginosuccinase. 4: Arginase
Linkage of urea & TCA cycle And Compartmentation of urea cycle
REGULATION OF UREA CYCLE
Metabolic disorders of Urea cycle
Treatment of disorder of urea cycle
TRANSMETHYLATION
DECARBOXYLATION
METABOLISM OF PHENYLALANINE
Glycogenic and ketogenic amino acids
A glucogenic amino acid is an amino acid that can be converted
into glucose through gluconeogenesis.This is in contrast to
the ketogenic amino acids, which are converted into ketone
bodies.
The production of glucose from glucogenic amino acids involves
these amino acids being converted to alpha keto acids and then
to glucose, with both processes occurring in the liver. This
mechanism predominates during catabolysis, rising
as fasting and starvation increase in severity.
In humans, the glucogenic amino acids are:
Alanine, Arginine, Asparagine, Aspartic acid, Cysteine, Glutamic
acid, Glutamine,
A ketogenic amino acid is an amino acid that can be degraded
directly into acetyl-CoA, which is the precursor of ketone
bodies and "myelin, especially during early development,
when brain myelin synthesis is extremely high” according to
the National institute of Health.[1] This is in contrast to
the glucogenic amino acids, which are converted into glucose.
Ketogenic amino acids are unable to be converted to glucose
as both carbon atoms in the ketone body are ultimately
degraded to carbon dioxide in the citric acid cycle.
In humans, two amino acids are exclusively ketogenic:
(remembered as all the "L" amino acids)
Leucine Lysine Glycine, Histidine, Methionine, Proline, Serine
and Valine.

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