Alpha-ketoglutarate-dependent sulfate ester dioxygenase (AtsK)

Alpha-ketoglutarate-dependent sulfate ester dioxygenase, commonly known as AtsK, is a non-heme iron(II)-dependent enzyme primarily identified in bacteria such as Pseudomonas putida (UniProt: P0A107). It functions within the sulfur starvation response (ssi) regulon, enabling the organism to utilize secondary sulfur sources when inorganic sulfate is scarce (Müller et al., 2004, Biochemistry). The enzyme catalyzes the oxidative desulfonation of alkyl sulfate esters, converting them into an aldehyde and inorganic sulfate while simultaneously decarboxylating alpha-ketoglutarate to succinate and CO2 (EC 1.14.11.25, BRENDA). Structurally, it belongs to the Fe(II)/alpha-ketoglutarate-dependent dioxygenase superfamily, characterized by a double-stranded beta-helix (DSBH) fold. Currently, AtsK is not recognized as a therapeutic target for clinical pharmacotherapy and has no known interacting drugs or established roles in human disease. Its significance is largely confined to microbial biochemistry and potential biotechnological applications in bioremediation for the degradation of sulfate-containing surfactants.

Other names

AtsKAlkylsulfataseAlpha-ketoglutarate-dependent alkylsulfataseAlkyl-sulfate, 2-oxoglutarate:oxygen oxidoreductase

The enzyme catalyzes the oxidative cleavage of the C-O bond in alkyl sulfate esters, producing the corresponding aldehyde and inorganic sulfate, coupled with the oxidative decarboxylation of alpha-ketoglutarate to succinate and carbon dioxide.