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).
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Isomerases / chemistry
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Amino Acid Isomerases / isolation & purification
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Amino Acid Isomerases / metabolism*
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Catalysis / drug effects
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Clostridium / enzymology*
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Electrophoresis, Polyacrylamide Gel
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Kinetics
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Molecular Weight
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Ornithine / metabolism*
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Pyridoxal Phosphate / metabolism
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Pyridoxal Phosphate / pharmacology
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Racemases and Epimerases / chemistry
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Racemases and Epimerases / isolation & purification*
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Racemases and Epimerases / metabolism*
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Spectrophotometry, Ultraviolet
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Substrate Specificity
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Thermodynamics
Substances
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Pyridoxal Phosphate
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Ornithine
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Racemases and Epimerases
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Amino Acid Isomerases
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ornithine racemase