Studies on Vitamin B6 Metabolism in Microorganisms Part X

Abstract

An enzyme, pyridoxamine 5•L-phosphate transaminase, was purified from the cell-free extract of Clostridium kainantoi. The purification procedures involved ammonium sulfate V. TANI, M. UKITA and K. OGATA

Evolutionary origin and functional diversification of aminotransferases

“…Pyridoxamine:pyruvate aminotransferase (PM-AT; EC 2.6.1.30) and pyridoxamine 5′-phosphate (PMP):α-ketoglutarate aminotransferase (PMP-AT; EC 2.6.1.54), so far found in bacteria ( i.e. , Mesorhizobium loti ( 65 ) and Clostridium kainantoi ( 95 )) and plant ( i.e. , Nicotiana tabacum ( 66 )), catalyze reversible transamination reactions between vitamin B 6 and keto acids in the absence of PLP.…”