Purification and properties of a novel sulfatase from Pseudomonas testosteroni that hydrolyzed 3 beta-hydroxy-5-cholenoic acid 3-sulfate.
A novel sulfatase hydrolyzing the sulfate ester bond in 3 beta-hydroxy-5-cholenoic acid 3-sulfate (delta 5-3 beta-sulfate) was purified from Pseudomonas testosteroni ATCC 11996 as the second bile acid sulfatase. The molecular weight was 95,000 and the molecule was composed of a homodimer of a subunit of which the molecular weight was 46,000. This sulfatase hydrolyzed delta 5-3 beta-sulfate to 3 alpha-hydroxy-5-cholenoic acid and sulfuric acid with inversion of beta- to alpha-configuration of the hydroxyl group at the C-3 position of the substrate. The optimum pH and the stable pH of the enzyme were 8.5 and 6.5-9.7, respectively. 3 beta-Sulfate ester bonds of steroids such as isolithocholic acid, pregnenolone, and epiandrosterone, in which the side chain of the steroid ring was shorter than cholesterol, were also hydrolyzed to 3 alpha-hydroxyl compounds corresponding to each steroid compound and sulfuric acid. We tentatively named this novel enzyme bile acid 3 beta-sulfate sulfohydrolase (beta-BSS).
Tazuke
Y
Y
Kyoto Research Laboratories, Marukin Shoyu Co., Ltd., Kyoto, Japan.
Matsuda
K
K
Adachi
K
K
Tsukada
Y
Y
D001192:Arylsulfatases / Q000378:metabolism*; D002793:Cholic Acids / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007477:Ions; D007526:Isoelectric Point; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013431:Sulfates / Q000378:metabolism; D013696:Temperature
D002793:Cholic Acids; D007477:Ions; D013431:Sulfates; C014596:3 beta-hydroxy-delta 5-cholenic acid; C101025:bile acid 3alpha-sulfate sulfohydrolase; D001192:Arylsulfatases