Purification and characterization of the 1-3-propanediol dehydrogenase of Clostridium butyricum E5
2000; Elsevier BV; Volume: 27; Issue: 6 Linguagem: Inglês
10.1016/s0141-0229(00)00219-2
ISSN1879-0909
Autores Tópico(s)Enzyme Catalysis and Immobilization
Resumo1-3 PPD dehydrogenase (EC 1.1.1.202) was purified to homogeneity from Clostridium butyricum E5 grown anaerobically on glycerol in continuous culture. The native enzyme was estimated by gel filtration to have a molecular weight of 384 200 +/- 31 100 Da; it is predicted to exist as an octamer or a decamer of identical molecular weight subunits. When tested as a dehydrogenase, the enzyme was most active with 1-3 propane diol. In the physiological direction, 3-hydroxypropionaldehyde was the preferred substrate. The apparent K(m) values of the enzyme for 3-hydroxypropionaldehyde and NADH were 0.17 mM and 0.06 mM, respectively. The enzyme requires only Mn(2+) for full activity. The enzyme was found to have properties similar to those reported for Klebsellia pneumoniae, Citrobacter freundii, and Clostridium pasteurianum.
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