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Cloning of the Gene Encoding α-Methylserine Hydroxymethyltransferase fromAminobactersp. AJ110403 andEnsifersp. AJ110404 and Characterization of the Recombinant Enzyme
Author(s) -
Hiroyuki Nozaki,
Shinji Kuroda,
Kunihiko Watanabe,
Kenzo Yokozeki
Publication year - 2008
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.80255
Subject(s) - serine hydroxymethyltransferase , cloning (programming) , protein subunit , molecular cloning , enzyme , gene , recombinant dna , escherichia coli , biology , microbiology and biotechnology , biochemistry , serine , chemistry , peptide sequence , computer science , programming language
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).

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