Purification and properties of ornithine racemase from Clostridium sticklandii
Purification and properties of ornithine racemase from Clostridium sticklandii
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DOI：
10.1128/jb.182.7.2052-2054.2000
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发表时间：
2000-04-01
影响因子：
3.2
通讯作者：
Wu, SH
中科院分区：
文献类型：
--
作者：
Chen, HP;Lin, CF;Wu, SH
用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法从胶状梭菌中分离纯化了鸟氨酸消旋酶，这是已知的第一个对鸟氨酸高度专一性的消旋酶。这种依赖PLP的酶的M-r为92,000，对L-鸟氨酸的K-m为0.77+/-0.0 5 mm，k(CAT)为980+/-20 S(-1)。
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).