EC Explorer

1.14.11.77

alkyl sulfatase

a primary alkyl sulfate ester + 2-oxoglutarate + O₂ = an aldehyde + succinate + CO₂ + sulfate

atsK (gene name), α-ketoglutarate-dependent sulfate ester dioxygenase, 2-oxoglutarate-dependent sulfate ester dioxygenase, type II alkyl sulfatase

primary alkyl sulfate ester, 2-oxoglutarate:oxygen oxidoreductase (sulfate-hydrolyzing)

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. The type II sulfatases oxidize the C-H bond of the carbon next to the sulfate ester, using 2-oxoglutarate and oxygen as substrates. The resulting hemiacetal sulfate ester collapses, liberating inorganic sulfate and an alkyl aldehyde along with carbon dioxide and succinate. The enzymes often desulfate a broad spectrum of linear and branched-chain sulfate esters. The enzyme from Pseudomonas putida acts on a range of medium-chain alkyl sulfate esters, with chain lengths ranging from C₄ to C₁₂. cf. sulfatase EC 3.1.6.1, arylsulfatase (type I), EC 3.1.6.21, linear primary-alkylsulfatase, and EC 3.1.6.22, branched primary-alkylsulfatase.

created 2021