Purification and Properties of Ornithine Racemase from Clostridium sticklandii
AUTOR(ES)
Chen, Hao-Ping
FONTE
American Society for Microbiology
RESUMO
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 Mr of 92,000, with a Km for l-ornithine of 0.77 ± 0.05 mM and a kcat of 980 ± 20 s−1.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=101933Documentos Relacionados
- Fermentation of Ornithine by Clostridium sticklandii1
- Purification and characterization of Clostridium sticklandii D-selenocystine alpha, beta-lyase.
- Partial Purification and Properties of Ornithine Transcarbamoylase from Nostoc muscorum Kützing 1
- 2,4-Diaminovaleric Acid: an Intermediate in the Anaerobic Oxidation of Ornithine by Clostridium sticklandii1
- Purification and Properties of a Thermoactive Glucoamylase from Clostridium thermosaccharolyticum