1992 年 112 巻 4 号 p. 456-460
A novel type of sulfotransferase was purified from Klebsiella K-36, an intestinal bacterium of rat. The enzyme (Mr 160, 000) is composed of two subunits (Mr 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 0.66mM, respectively. The enzyme is activated by magnesium ion and inhibited by EDTA.