Properties of D-hydantoinase from Agrobacterium tumefaciens and its use for the preparation of N-carbamyl D-amino acids.

作者: D.R. Durham , J.E. Weber

DOI: 10.1006/BBRC.1995.2733

关键词: HydantoinRacemizationEnzymeStereochemistryChemistryStereospecificityChemical kineticsBiocatalysisAgrobacterium tumefaciensAmino acid

摘要: Agrobacterium tumefaciens strain 47C expresses an inducible D-hydantoinase that catalyzes the formation of optically pure N-carbamyl D-amino acids from racemic hydantoin precursors. The D-Hydantoinase was shown to be active and stable at elevated temperatures pH values, thus affording favorable bioreaction conditions result in racemization DL-hydantoins utilizable D-isomer. enzyme demonstrated optimal reaction kinetics 10 70°C, not activated by metal ions, exhibited a distinctive substrate specificity. A. hydantoinase most on 5,6-dihydrouracil DL-5-methylhydantoin with only slight activity DL-benzylhydantoin. Extracts or whole cells were used as biocatalyst mediate stereospecific conversion DL-phenylhydantoin respective acids. In addition, immobilized cell systems useful for reuse.

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