| Cloning and overexpression of ketopantoic acid reductase gene from Stenotrophomonas maltophilia and its application to stereospecific production of D: -pantoic acid. | |
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MedLine Citation:
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PMID: 22083276 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Ketopantoic acid (KPA) reductase catalyzes the stereospecific reduction of ketopantoic acid to D: -pantoic acid. Based on the N-terminal amino acid sequence of KPA reductase from Stenotrophomonas maltophilia 845, the KPA reductase gene was cloned from S. maltophilia NBRC14161 and sequenced. This gene contains an open reading frame of 777 bp encoding 258 amino acid residues, and the deduced amino acid sequence showed high similarity to the SDR superfamily proteins. An expression vector, pETSmKPR, containing the full KPA reductase gene was constructed and introduced into Escherichia coli BL21 (DE3) to overexpress the enzyme. Bioreduction of KPA using E. coli transformant cells coexpressing KPA reductase together with cofactor regeneration enzyme gene was also performed. The conversion yield of KPA to D: -pantoic acid reached over 88% with a substrate concentration up to 1.17 M. |
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Authors:
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Dayong Si; Nobuyuki Urano; Sakayu Shimizu; Michihiko Kataoka |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-15 |
Journal Detail:
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Title: Applied microbiology and biotechnology Volume: - ISSN: 1432-0614 ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-15 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8406612 Medline TA: Appl Microbiol Biotechnol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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