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.
Kim
D H
DH
College of Pharmacy, Kyung Hee University, Seoul, Korea.
Kim
H S
HS
Kobashi
K
K
D000818:Animals; D001426:Bacterial Proteins / Q000302:isolation & purification*; D004795:Enzyme Stability; D007422:Intestines / Q000382:microbiology*; D007700:Kinetics; D007709:Klebsiella / Q000201:enzymology*; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D051381:Rats; D017208:Rats, Wistar; D013379:Substrate Specificity; D013431:Sulfates / Q000378:metabolism; D015238:Sulfotransferases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D013431:Sulfates; D015238:Sulfotransferases