Purification and characterization of novel sulfotransferase obtained from Klebsiella K-36, an intestinal bacterium of rat.

A novel type of sulfotransferase was purified from Klebsiella K-36, an intestinal bacterium of rat. The enzyme (M(r) 160,000) is composed of two subunits (M(r) 73,000) with pI and optimal pH values of 5.3 and 10-10.5, respectively. The apparent Km for PNS (p-nitrophenyl sulfate) using phenol as an acceptor and that for phenol using PNS as a donor substrate were determined to be 0.11 and 0.66 mM, respectively. The enzyme is activated by magnesium ion and inhibited by EDTA.