Cloning of the gene encoding α-methylserine hydroxymethyltransferase from Aminobacter sp. AJ110403 and Ensifer sp. AJ110404 and characterization of the recombinant enzyme

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  • Cloning of the Gene Encoding .ALPHA.-Methylserine Hydroxymethyltransferase from Aminobacter sp. AJ110403 and Ensifer sp. AJ110404 and Characterization of the Recombinant Enzyme
  • Cloning of the gene encoding アルファ methylserine hydroxymethyltransferase from Aminobacter sp AJ110403 and Ensifer sp AJ110404 and characterization of the recombinant enzyme
  • 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

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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 Vmax 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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