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. 1977 Dec 1;167(3):843–846. doi: 10.1042/bj1670843

The mechanism of action of primary alkylsulphohydrolase and arylsulphohydrolase from a detergent-degrading micro-organism.

J M Cloves, K S Dodgson, D E Games, D J Shaw, G F White
PMCID: PMC1183735  PMID: 603638

Abstract

Previous studies have shown that secondary alkylsulphohydrolases from certain detergent-degrading micro-organisms are unusual esterases in that they catalyse fission of the C-O bond of the alkyl sulphate ester linkage. The position of bond fission catalysed by a primary alkylsulphatase and an arylsulphohydrolase present in Pseudomonas C12B has now been investigated. The primary alkylsulphatase behaved like the secondary alkylsulphohydrolases in cleaving the C-O bond of potassium heptan-1-yl sulphate. In contrast, the arylsulphohydrolase, in common with other similar enzymes previously studied, catalysed the fission of the O-S bond of potassium p-nitrophenyl sulphate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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