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The transfer of the amino group of an amino acid to a keto acid, usually α-ketoglutaric acid, to form glutamate and the keto acid derived from the original amino acid. Transamination reactions are catalysed by transaminases, such as aspartate transaminase, which catalyses the reversible formation of oxaloacetic acid and glutaric acid from aspartic acid and α-ketoglutaric acid.
Transamination is central to amino-acid metabolism as it is one of the steps in the biosynthesis and the degradation of nearly all amino acids.
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