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One of a group of enzymes that catalyze the transfer of the amino group of an amino acid to a keto acid to form another amino acid. Also known as aminotransferase.



(also aminotransferase and aminopherase), an enzyme of the transferase group that catalyzes the transfer of an amino group (—NH2) from an α-amino acid to an α-keto acid. Transaminases are found in most animal and plant tissues and play an important part in nitrogen metabolism. The role of transaminase in the transamination process was discovered by the Soviet biochemists A. E. Braunshtein and M. G. Kritsman in 1937. The coenzyme in transaminase reactions is pyridoxal phosphate, the aldehyde group of which serves as intermediate acceptor of the amino group. The resulting pyridoxamine phosphate transfers the amino group to the ketone group of the acid undergoing amination. The reaction is reversible.


References in periodicals archive ?
The first serum marker [serum glutamic-oxaloacetic transaminase (SGOT), also known as aspartate transaminase (AST)] to facilitate the diagnosis of myocardial infarction (MI) was described in 1954.
3 The patients liver-function profile showed a serum glutamic-oxaloacetic transaminase (SGOT) of 111 U/L (normal range 0 to 40 U/L) and a lactate dehydrogenase (LDH)of 231 U/L (normal range CA to 165 U/L).
Serum glutamic-oxaloacetic transaminase and glutamic-pyruvic transaminase were measured by the IFCC method (Hitachi 917[R] device, Roche Diagnostics, Florida, USA).

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