Document Detail


Lysine racemase from a lactic acid bacterium, Oenococcus oeni: Structural basis of substrate specificity.
MedLine Citation:
PMID:  23035128     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Shiro Kato; Hisashi Hemmi; Tohru Yoshimura
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-3
Journal Detail:
Title:  Journal of biochemistry     Volume:  -     ISSN:  1756-2651     ISO Abbreviation:  J. Biochem.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-4     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-Ku, Nagoya, Aichi 464-8601, Japan.
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