Transamination of l-cystathionine and related compounds by bovine brain glutamine transaminase.
Glutamine transaminase (EC 2.6.1.15) has been purified 113 fold from bovine brain. The product is free of aspariate amino transferase (EC 2.6.1.1.) and other common transaminases. The enzyme shows a wide specificity similar to that reported from the same transaminase purified from bovine kidney and liver as regards both the amino donor and the amino acceptor. Of interest is the transamination and cyclization of l-cystathionine, l-lanthionine, l-cystine and S-aminoethylcysteine. The latter result indicates that the deamination and the cyclization of the sulfur containing diamino acids described for bovine liver and kidney enzyme is feasible also in the brain and suggests the possible endogenous origin of cyclothionine and thiomorpholine dicarboxylate recently detected in bovine brain.
Costa
M
M
Department of Biochemical Sciences, University of Rome "La Sapienza" and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Piazzale Aldo Moro 5, 00185-Rome, Italy.
Pensa
B
B
Di Costanzo
B
B
Coccia
R
R
Cavallini
D
D