On the Two Components of Pyridoxal 5′-Phosphate Synthase from Bacillus subtilis

摘要: Vitamin B6 is an essential nutrient in the human diet. It can act as a co-enzyme for numerous metabolic enzymes and has recently been shown to be potent antioxidant. Plants microorganisms have ability make compound. Yet, studies of vitamin biosynthesis mainly restricted Escherichia coli, where synthesized from 1-deoxy-d -xylulose 5-phosphate 4-phosphohydroxy-l-threonine. Recently, novel pathway its synthesis discovered, involving two genes (PDX1 PDX2) neither which homologous any those participating E. coli pathway. In Bacillus subtilis, YaaD YaaE represent PDX1 PDX2 homolog, respectively. The proteins form complex that functions glutamine amidotransferase, with glutaminase domain acceptor pyridoxal 5'-phosphate (PLP) domain. this report we corroborate recent on identification substrates provide unequivocal proof identity reaction product. We show both synthase reactions are dependent respective protein partner. also utilize external ammonium source but, contrast other amidotransferases, under certain conditions. Furthermore, detailed characterization inhibition domain, thus PLP synthesis, by analog acivicin. Employing pull-out assays native-PAGE, evidence dissociation bi-enzyme these results discussed light nature interaction components enzyme complex.