TAILIEUCHUNG - Báo cáo khoa học: Isolation and molecular characterization of a novel D-hydantoinase from Jannaschia sp. CCS1

Hydantoinases (HYDs) are important enzymes for industrial production of optically pure amino acids, which are widely used as precursors for various semi-synthetic antibiotics. By a process coupling genomic data mining with activity screening, a new hydantoinase, tentatively designated HYDJs, was identified from Jannaschiasp. CCS1 and overexpressed in Escherichia coli. | ỊFEBS Journal Isolation and molecular characterization of a novel D-hydantoinase from Jannaschia sp. CCS1 Yuanheng Cai1 Peter Trodler2 Shimin Jiang1 Weiwen Zhang3 Yan Wu1 Yinhua Lu1 Sheng Yang1 and Weihong Jiang1 4 1 Key Laboratory of Synthetic Biology Institute of Plant Physiology and Ecology Shanghai Institutes for BiologicalSciences Chinese Academy of Sciences Shanghai China 2 Institute of TechnicalBiochemistry University of Stuttgart Germany 3 Center for Ecogenomics Biodesign Institute Arizona State University Tempe AZ USA 4 Institut Pasteur of Shanghai Chinese Academy of Sciences Shanghai China Keywords hydantoinase Jannaschia sp. CCS1 saturated mutagenesis structural analysis substrate binding pocket Correspondence W. Jiang Key Laboratory of Synthetic Biology Institute of Plant Physiology and Ecology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Shanghai 200032 China Fax 86 21 54924015 Tel 86 21 54924172 E-mail whjiang@ Received 4 February 2009 revised 15 April 2009 accepted 27 April 2009 doi Hydantoinases HYDs are important enzymes for industrial production of optically pure amino acids which are widely used as precursors for various semi-synthetic antibiotics. By a process coupling genomic data mining with activity screening a new hydantoinase tentatively designated HYDJs was identified from Jannaschia sp. CCS1 and overexpressed in Escherichia coli. The specific activity of HYDJs on D L-p-hydroxyphenylhydantoin as the substrate was three times higher than that of the hydantoinase originating from Burkholderia pickettii HYDBp that is currently used in industry. The enzyme obtained was a homotetramer with a molecular mass of 253 kDa. The pH and temperature optima for HYDJs were and 50 C respectively similar to those of HYDBp. Kinetic analysis showed that HYDJs has a higher kcat value on D L-p-hydroxyphenylhydantoin than HYDBp does. Homology modeling and substrate docking analyses of .

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