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Transaminase

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transaminase [¦tranz′am·ə‚nās]
(biochemistry)
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.

Transaminase 

(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.

A. A. BOLDYREV



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The Schiff's bases and their metal complexes of the present invention are useful for the modulation of metal-activated enzymes and metalloenzymes, such as Phenylalanine Hydroxylase, Tyrosine Transaminase, Phenylalanine Transaminase, Tyrosinase, various MMP (Matrix metalloproteases), Superoxide dismutase, 5-Alpha Reductase, and citrate lyase.
Serial transaminase measurements provide a noninvasive means of estimating the severity of hepatitis C virus infection in infected renal transplant recipients and make liver biopsy unnecessary, according to researchers at the University of Istanbul, Turkey.
 
 
 
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