Purification and properties of ornithine racemase from Clostridium sticklandii |
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| Authors: | Chen H P Lin C F Lee Y J Tsay S S Wu S H |
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| Affiliation: | Department of Biochemistry, China Medical College, Taichung 404, Taiwan. hpchen@mail.cmc.edu |
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| 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). |
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