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EC 3.1.6.19 Details
EC number
3.1.6.19
Accepted name
(R)-specific secondary-alkylsulfatase (type III)
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, (R)-specific secondary-alkylsulfatase, type III (R)-specific secondary-alkylsulfatase
Systematic name
(R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol-forming]
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-β-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
created 2013, modified 2021
EC Tree
1.1.1.68 created 1965, deleted 1978 [transferred to EC 1.1.99.15, deleted 1980]
1.1.1.70 created 1965, deleted 1978
1.1.1.74 created 1972, deleted 1976
1.1.1.89 created 1972, deleted 1976
1.1.1.109 created 1972, deleted 1976
1.1.1.139 created 1972, deleted 1978
1.1.1.155 created 1976, deleted 2004
1.1.1.171 created 1978, deleted 1984
1.1.1.180 created 1983, deleted 1984
1.1.1.182 created 1983, deleted 1990
1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004
1.1.1.242 created 1992, deleted 2001
1.1.1.249 provisional version created 1999, deleted 1999 (reinstated 2001 as EC 2.5.1.46)
1.1.1.253 created 1999, deleted 2003