Purification and Properties of -Hydroxybutyrate Dehydrogenase from Mycobacterium phlei ATCC354
Open Access
- 1 January 1978
- journal article
- research article
- Published by Microbiology Society in Journal of General Microbiology
- Vol. 104 (1) , 123-126
- https://doi.org/10.1099/00221287-104-1-123
Abstract
β-Hydroxybutyrate dehydrogenase (EC 1.1.1.30) was purified 145-fold from Mycobacterium phlei ATCC354 by ammonium sulphate fractionation and DEAE-cellulose chromatography. The pH optima for oxidation and reduction reactions were 8.4 and 6.8 respectively. The purified enzyme was specific for NAD, NADH, acetoacetate and D(-)-β-hydroxybutyrate. Km values for DL-β-hydroxybutyrate and NAD were 7.4 mM and 0.66 mM respectively. The enzyme was inactivated by mercurial thiol inhibitors and by heat, but could be protected by NADH, Ca2+ and partially by Mn2+. The enzyme did not require metal ions and was insensitive to EDTA, glutathione, dithiothreitol, β-mercaptoethanol and cysteine.Keywords
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