The Enzyme Database

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Accepted name: alkyl sulfatase
Reaction: a primary alkyl sulfate ester + 2-oxoglutarate + O2 = an aldehyde + succinate + CO2 + sulfate
Other name(s): atsK (gene name); α-ketoglutarate-dependent sulfate ester dioxygenase; 2-oxoglutarate-dependent sulfate ester dioxygenase; type II alkyl sulfatase
Systematic name: primary alkyl sulfate ester, 2-oxoglutarate:oxygen oxidoreductase (sulfate-hydrolyzing)
Comments: 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, arylsulfatase (type I), EC, linear primary-alkylsulfatase, and EC, branched primary-alkylsulfatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Kahnert, A. and Kertesz, M.A. Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313. J. Biol. Chem. 275 (2000) 31661–31667. [DOI] [PMID: 10913158]
2.  Muller, I., Kahnert, A., Pape, T., Sheldrick, G.M., Meyer-Klaucke, W., Dierks, T., Kertesz, M. and Uson, I. Crystal structure of the alkylsulfatase AtsK: insights into the catalytic mechanism of the Fe(II) α-ketoglutarate-dependent dioxygenase superfamily. Biochemistry 43 (2004) 3075–3088. [DOI] [PMID: 15023059]
3.  Sogi, K.M., Gartner, Z.J., Breidenbach, M.A., Appel, M.J., Schelle, M.W. and Bertozzi, C.R. Mycobacterium tuberculosis Rv3406 is a type II alkyl sulfatase capable of sulfate scavenging. PLoS One 8:e65080 (2013). [DOI] [PMID: 23762287]
[EC created 2021]

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