A novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae

YGL196W of Saccharomyces cerevisiae encodes a putative protein that is unidentified but is predicted to have a motif similar to that of the N-terminal domain of the bacterial alanine racemase. In the present study we found that YGL196W encodes a novel D-serine dehydratase, which belongs to a differe...

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Veröffentlicht in:	Biochemical journal 2008-01, Vol.409 (2), p.399-406
Hauptverfasser:	Ito, Tomokazu, Hemmi, Hisashi, Kataoka, Kunishige, Mukai, Yukio, Yoshimura, Tohru
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Edetic Acid - pharmacology Enzyme Stability Escherichia coli Escherichia coli - genetics Hydro-Lyases - chemistry Hydro-Lyases - isolation & purification Hydro-Lyases - metabolism Hydrogen-Ion Concentration Isomerism Kinetics Molecular Sequence Data Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - isolation & purification Saccharomyces cerevisiae Proteins - metabolism Stereoisomerism Substrate Specificity Temperature Zinc - pharmacology
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