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

Hiroyuki NOZAKI; Shinji KURODA; Kunihiko WATANABE; Kenzo YOKOZEKI

doi:10.1271/bbb.80255

This article has now been updated. Please use the final version.

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

Hiroyuki NOZAKI, Shinji KURODA, Kunihiko WATANABE, Kenzo YOKOZEKI

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Keywords: α-methylserine hydroxymethyltransferase, pyridoxal 5′-phosphate, tetrahydrofolate, Aminobacter, Ensifer

JOURNAL FREE ACCESS Advance online publication

Article ID: 80255

DOI https://doi.org/10.1271/bbb.80255

The final version of this article is now available: Vol. 72 (2008) , No. 11 p.3002

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Abstract

Genes encoding α-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 α-methyl-L-serine to D-alanine via tetrahydrofolate was 22.1 U/mg (AJ110403) and 15.4 U/mg (AJ110404).

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