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Genes encoding alpha-methylserine hydroxymethyltransferase from Aminobacter sp. AJ110403 and Ensifer sp. AJ110404 were cloned and expressed in Escherichia coli. The purified enzymes were homodimers with a 46-kDa subunit and contained 1 mol/mol-subunit of pyridoxal 5'-phosphate. The V(max) of these enzymes catalyzing the conversion of alpha-methyl-L-serine to D-alanine via tetrahydrofolate was 22.1 U/mg (AJ110403) and 15.4 U/mg (AJ110404).

bioscience, biotechnology, and biochemistry

Cloning of the Gene Encoding α-Methylserine Hydroxymethyltransferase from<i>Aminobacter</i>sp. AJ110403 and<i>Ensifer</i>sp. AJ110404 and Characterization of the Recombinant Enzyme

Cloning of the Gene Encoding α-Methylserine Hydroxymethyltransferase fromAminobactersp. AJ110403 andEnsifersp. AJ110404 and Characterization of the Recombinant Enzyme