Occurrence, purification and properties of the staphylococcal beta-hydroxybutyrate dehydrogenase.
beta-Hydroxybutyrate dehydrogenase (EC 1.1.1.30.)-an enzyme involved in degradation of polymer store material-was found in staphylococci. The enzyme was isolated from Staphylococcus xylosus NCTC D100694 cells, purified and characterized. The native enzyme is a tetramer and consists of equal subunits. Its relative molecular mass is M(r) = 140 kDa and pI = 4.7. The enzyme activity is stimulated by Mg+2 and Ca+2 ions. Staphylococcal beta-hydroxybutyrate dehydrogenase is relatively stable and active in a wide temperature range. The optimum pH for oxidation is 8.6 and for reduction 6.7. The enzyme is highly specific for D(-)stereoisomer of beta-hydroxybutyrate. Km values for beta-hydroxybutyrate and acetoacetate are 39.1 microM and 5.47 microM, respectively.
Szewczyk
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Department of Pharmaceutical Microbiology, Medical University, Lódź, Poland.
Rózalska
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M
D000090:Acetoacetates / Q000378:metabolism; D002412:Cations / Q000494:pharmacology; D004795:Enzyme Stability; D006884:Hydroxybutyrate Dehydrogenase / Q000737:chemistry / Q000187:drug effects / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013045:Species Specificity; D013210:Staphylococcus / Q000201:enzymology*
D000090:Acetoacetates; D002412:Cations; C016635:acetoacetic acid; D006884:Hydroxybutyrate Dehydrogenase