|
type |
Journal Article |
authors |
Kato S, Hemmi H, Yoshimura T |
title |
Lysine racemase from a lactic acid bacterium, Oenococcus oeni: structural basis of substrate specificity |
journal |
J Biochem |
Activity |
5.1.1.5 |
Family |
5.1.1.5.b |
sel |
selected |
ui |
23035128 |
year |
(2012) |
volume |
152 |
number |
6 |
pages |
505-8 |
| |
keywords |
doi: 10.1093/jb/mvs120 |
abstract |
Oenococcus oeni, a lactic acid bacterium, possesses a lysine racemase, which has a specific activity towards 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, whereas I222T/Y354W double mutations endowed alanine racemase with lysine racemization activity. These results suggest that the two residues play an important role in lysine racemization. |
last changed |
2017/12/12 10:11 |
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