Purification and properties of ornithine racemase from Clostridium sticklandii

J Bacteriol. 2000 Apr;182(7):2052-4. doi: 10.1128/JB.182.7.2052-2054.2000.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Isomerases / chemistry
  • Amino Acid Isomerases / isolation & purification
  • Amino Acid Isomerases / metabolism*
  • Catalysis / drug effects
  • Clostridium / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Kinetics
  • Molecular Weight
  • Ornithine / metabolism*
  • Pyridoxal Phosphate / metabolism
  • Pyridoxal Phosphate / pharmacology
  • Racemases and Epimerases / chemistry
  • Racemases and Epimerases / isolation & purification*
  • Racemases and Epimerases / metabolism*
  • Spectrophotometry, Ultraviolet
  • Substrate Specificity
  • Thermodynamics

Substances

  • Pyridoxal Phosphate
  • Ornithine
  • Racemases and Epimerases
  • Amino Acid Isomerases
  • ornithine racemase