Purification and properties of a novel sulfatase from Pseudomonas testosteroni that hydrolyzed 3 beta-hydroxy-5-cholenoic acid 3-sulfate.

Y Tazuke, K Matsuda, K Adachi, Y Tsukada

Index: Biosci. Biotechnol. Biochem. 62(9) , 1739-44, (1998)

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Abstract

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).