E. Szewczyk et M. Rozalska, OCCURRENCE, PURIFICATION AND PROPERTIES OF THE STAPHYLOCOCCAL BETA-HYDROXYBUTYRATE DEHYDROGENASE, Acta Microbiologica Polonica, 43(1), 1994, pp. 33-45
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 cel
ls, purified and characterized. The native enzyme is a tetramer and co
nsists of equal subunits. Its relative molecular mass is M(r) = 140 kD
a and pI = 4.7. The enzyme activity is stimulated by Mg+2 and Ca+2 ion
s. Staphylococcal beta-hydroxybutyrate dehydrogenase is relatively sta
ble and active in a wide temperature range. The optimum pH for oxidati
on is 8.6 and for reduction 6.7. The enzyme is highly specific for D(-
)stereoisomer of beta-hydroxybutyrate. K(m) values for beta-hydroxybut
yrate and acetoacetate are 39.1 muM and 5.47 muM, respectively.