The Enzyme Database

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Accepted name: (R)-specific secondary-alkylsulfatase
Reaction: an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate
Other name(s): S3 secondary alkylsulphohydrolase; Pisa1; secondary alkylsulphohydrolase; (R)-specific sec-alkylsulfatase; sec-alkylsulfatase
Systematic name: (R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol forming]
Comments: The enzyme from Rhodococcus ruber is involved in the biodegradation of alkyl sulfate esters used as detergents and released into the environment. The prefered substrates are linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates [1]. The enzyme from Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Perfect enantioselectivities are obtained for substrates bearing groups of different size adjacent to the sulfate moiety [4]. The enzymic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom [1,4]. The enzyme contains a Zn2+ ion [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Pogorevc, M. and Faber, K. Purification and characterization of an inverting stereo- and enantioselective sec-alkylsulfatase from the gram-positive bacterium Rhodococcus ruber DSM 44541. Appl. Environ. Microbiol. 69 (2003) 2810–2815. [PMID: 12732552]
2.  Wallner, S.R., Nestl, B.M. and Faber, K. Highly enantioselective sec-alkyl sulfatase activity of Sulfolobus acidocaldarius DSM 639. Org. Lett. 6 (2004) 5009–5010. [PMID: 15606122]
3.  Knaus, T., Schober, M., Kepplinger, B., Faccinelli, M., Pitzer, J., Faber, K., Macheroux, P. and Wagner, U. Structure and mechanism of an inverting alkylsulfatase from Pseudomonas sp. DSM6611 specific for secondary alkyl sulfates. FEBS J. 279 (2012) 4374–4384. [PMID: 23061549]
4.  Schober, M., Knaus, T., Toesch, M., Macheroux, P., Wagner, U. and Faber, K. The substrate spectrum of the inverting sec-alkylsulfatase Pisa1. Adv. Synth. Catal. 354 (2012) 1737–1742.
[EC created 2013]

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