| Lysine racemase from a lactic acid bacterium, Oenococcus oeni: Structural basis of substrate specificity. | |
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MedLine Citation:
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PMID: 23035128 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Oenococcus oeni, a lactic acid bacterium, possesses a lysine racemase, which has a specific activity toward basic amino acids. A comparison of amino acid residues around the active site suggested that Ile222 and Tyr354 of the Geobacillus stearothermophilus alanine racemase, which shares 60% sequence similarity with lysine racemase, were replaced by Thr224 and Trp355 in the O. oeni lysine racemase. T224I/W355Y double mutations significantly decreased the activity of lysine racemase, while I222T/Y354W double mutations endowed alanine racemase with lysine racemization activity. These results suggest that the 2 residues play an important role in lysine racemization. |
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Authors:
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Shiro Kato; Hisashi Hemmi; Tohru Yoshimura |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-3 |
Journal Detail:
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Title: Journal of biochemistry Volume: - ISSN: 1756-2651 ISO Abbreviation: J. Biochem. Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0376600 Medline TA: J Biochem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-Ku, Nagoya, Aichi 464-8601, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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