PROTEIN METABOLISM
General Reactions of Aminoacids
Demination
Deamidation
Transamination
Decarboxylation
TRANSAMINATION
Aminoacid Amino group donor
Keto asit (Product)
Aminoacid (Product) Keto acid Amino group acceptor
Glutamate + α-keto acide α-keto glutarate + α-aminoacid ↔
TRANSAMINASES
Transamination reactions are controlled by enzymes called transaminases.
Each transaminase is specific for one or more amino group donors.
Two important transaminase reactions are catalyzed by alanine aminotransferase (ALT) and aspartate aminotransferase (AST).
Glutamate + Pyruvate ↔ Alanine + alpha keto glutarate
Alanine transaminase (ALT)
https://www.sciencedirect.com/topics/neuroscience/transamination
DEAMINATION
Deamination of amino acids →→ Formation of the carbon skeletons of
alpha-keto acids
OXİDATIVE DEAMINATION
NAD(P) NAD(P)H + H
+Glutamate + H
2O Alpha ketoglutarate + NH
4+L-Aminoacid + O
2Alpha ketoacid + NH
4++ H
2O
2L-Aminoacid oxidase
Glutamate dehydrogenase
DEAMIDATION
Glutaminase
Glutamate + NH
4+Glutamine
DECARBOXYLATION
Decarboxylation results in carbon dioxide release
There are many amino acid decarboxylases.
They convert amino acids into biogenic amines and carbon dioxide.
Histidin →Histamin
Fenil alanin → Dopamin
Tryptophane → Tryptamine
Aspartate → Beta Alanine
Glutamate → GABA
UREA
C O
NH
2NH
2 It is produced by the liver
It is transported to the kidneys through the blood
It is excreted by the urine.
NH
3+ + 3 ATP + Aspartate
Urea + Fumarate + 2 ADP +AMP + 2Pi + PPi
UREA CYCLE
H
2O +
HCO
3-REFERENCES
Lippincott’s Illustrated Reviews Biochemistry Denise R. Ferrier Series Editor: Richard A. Harvey, 6th Edition https://www.ncbi.nlm.nih.gov/pubmed/22139560