| Purification and characterization of a cis-epoxysuccinic acid hydrolase from Nocardia tartaricans CAS-52, and expression in Escherichia coli. | |
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MedLine Citation:
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PMID: 22552902 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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A highly enantioselective cis-epoxysuccinic acid hydrolase from Nocardia tartaricans was purified to electrophoretic homogeneity. The enzyme was purified 184-fold with a yield of 18.8 %. The purified cis-epoxysuccinic acid hydrolase had a monomeric molecular weight of 28 kDa, and its optimum conditions were 37 °C and pH 7-9. With sodium cis-epoxysuccinate as the substrate, Michaelis-Menten enzyme kinetics analysis gave a Km value of 35.71 mM and a Vmax of 2.65 mM min(-1). The enzyme was activated by Ni(2+) and Al(3+), while strongly inhibited by Fe(3+), Fe(2+), Cu(2+), and Ag(+). The cis-epoxysuccinic acid hydrolase gene was cloned, and its open reading frame sequence predicted a protein composed of 253 amino acids. A pET11a expression plasmid carrying the gene under the control of the T7 promoter was introduced into Escherichia coli, and the cis-epoxysuccinic acid hydrolase gene was successfully expressed in the recombinant strains. |
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Authors:
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Ziqiang Wang; Yunshan Wang; Zhiguo Su |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-5-3 |
Journal Detail:
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Title: Applied microbiology and biotechnology Volume: - ISSN: 1432-0614 ISO Abbreviation: - Publication Date: 2012 May |
Date Detail:
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Created Date: 2012-5-3 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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National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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