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PMID: 10715017 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and properties of ornithine racemase from Clostridium sticklandii.

Journal of bacteriology ·Vol. 182 ·No. 7 ·2000-04-00 ·Pages 2052-4

Chen HP, Lin CF, Lee YJ, Tsay SS, Wu SH

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).

MeSH Terms
Amino Acid Isomerases/chemistry,isolation & purification,metabolism Catalysis/drug effects Clostridium/enzymology Electrophoresis, Polyacrylamide Gel Kinetics Molecular Weight Ornithine/metabolism Pyridoxal Phosphate/metabolism,pharmacology Racemases and Epimerases/chemistry,isolation & purification,metabolism Spectrophotometry, Ultraviolet Substrate Specificity Thermodynamics
Chemicals
Pyridoxal Phosphate Ornithine Racemases and Epimerases Amino Acid Isomerases ornithine racemase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Chen H P
Department of Biochemistry, China Medical College, Taichung 404, Taiwan. hpchen@mail.cmc.edu
Lin C F
Lee Y J
Tsay S S
Wu S H
References (8)
8 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.182.7.2052-2054.2000
Email
hpchen@mail.cmc.edu
Published
2000-04-00
Pages
2052-4
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC101933
Subset
IM
External Links
PubMed source DOI: 10.1128/JB.182.7.2052-2054.2000 PMC Full Text View journal details
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