|
type |
Journal Article |
authors |
Chen, H. P.; Lin, c. f.; Lee, Y.J.; Tsay, S.S.; Wu S.H. |
title |
Purification and properties of ornithine racemase from Clostridium sticklandii |
journal |
J Bacteriol |
Activity |
5.1.1.12 |
Family |
5.1.1.12 |
sel |
selected |
ui |
10715017 |
year |
(2000) |
volume |
182 |
number |
7 |
pages |
2052-4 |
| |
keywords |
Amino Acid Motifs |
abstract |
Ornithine racemase has been purified to homogeneity from Clostridium sticklandii, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This is the first racemase known to be highly specific to ornithine. This PLP-dependent enzyme has an M(r) of 92, 000, with a K(m) for L-ornithine of 0.77 +/- 0.05 mM and a k(cat) of 980 +/- 20 s(-1). |
last changed |
2017/12/15 12:02 |
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