KEGG   ENZYME: 3.1.6.19
Entry
EC 3.1.6.19                 Enzyme                                 

Name
(R)-specific secondary-alkylsulfatase (type III);
S3 secondary alkylsulphohydrolase;
Pisa1;
secondary alkylsulphohydrolase;
(R)-specific sec-alkylsulfatase;
sec-alkylsulfatase;
(R)-specific secondary-alkylsulfatase;
type III (R)-specific secondary-alkylsulfatase
Class
Hydrolases;
Acting on ester bonds;
Sulfuric-ester hydrolases
Sysname
(R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol-forming]
Reaction(IUBMB)
an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate
Substrate
(R)-secondary-alkyl sulfate;
H2O [CPD:C00001]
Product
(S)-secondary-alcohol;
sulfate [CPD:C00059]
Comment
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-beta-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. The enzyme from the bacterium Rhodococcus ruber prefers linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates [1]. The enzyme from the bacterium Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom, resulting in perfect enantioselectivity. cf. EC 3.1.6.1, arylsulfatase (type I), and EC 1.14.11.77, alkyl sulfatase (type II).
History
EC 3.1.6.19 created 2013, modified 2021
Reference
1  [PMID:12732552]
  Authors
Pogorevc M, Faber K
  Title
Purification and characterization of an inverting stereo- and enantioselective sec-alkylsulfatase from the gram-positive bacterium Rhodococcus ruber DSM 44541.
  Journal
Appl Environ Microbiol 69:2810-5 (2003)
DOI:10.1128/AEM.69.5.2810-2815.2003
Reference
2  [PMID:15606122]
  Authors
Wallner SR, Nestl BM, Faber K
  Title
Highly enantioselective sec-alkyl sulfatase activity of Sulfolobus acidocaldarius DSM 639.
  Journal
Org Lett 6:5009-10 (2004)
DOI:10.1021/ol0477778
Reference
3  [PMID:23061549]
  Authors
Knaus T, Schober M, Kepplinger B, Faccinelli M, Pitzer J, Faber K, Macheroux P, Wagner U
  Title
Structure and mechanism of an inverting alkylsulfatase from Pseudomonas sp. DSM6611 specific for secondary alkyl sulfates.
  Journal
FEBS J 279:4374-84 (2012)
DOI:10.1111/febs.12027
Reference
4
  Authors
Schober, M., Knaus, T., Toesch, M., Macheroux, P., Wagner, U. and Faber, K.
  Title
The substrate spectrum of the inverting sec-alkylsulfatase Pisa1.
  Journal
Adv Synth Catal 354:1737-1742 (2012)
Other DBs
ExplorEnz - The Enzyme Database: 3.1.6.19
IUBMB Enzyme Nomenclature: 3.1.6.19
ExPASy - ENZYME nomenclature database: 3.1.6.19
BRENDA, the Enzyme Database: 3.1.6.19

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