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. 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 C(4) to C(12). 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.
2-oxoglutarate-dependent sulfate ester dioxygenase, alpha-ketoglutarate-dependent sulfate ester dioxygenase, AtsK, Rv3406, type II alkyl sulfatase, more
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. 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 C(4) to C(12). 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.
2-keto acids support desulfation at the following rates, relative to the rate obtained with 2-oxoglutarate: 2-oxo-valerate 87%, 2-oxo-adipate 81%, 2-oxo-octanoate 31%, 3-methyl-2-oxo-butyrate 25%, and oxaloacetate 15%. No desulfation is obtained with pyruvate
AtsK protein catalyzes the alpha-ketoglutarate-dependent cleavage of a range of alkyl sulfate esters, with chain lengths ranging from C4 to C12, requires oxygen and Fe2+ for activity and releases succinate, sulfate, and the corresponding aldehyde as products
an enzyme deletion mutant strain does not replicate in minimal media with 2-ethyl hexyl sulfate as the sole sulfur source, in contrast to wild type or the complemented strain
an enzyme deletion mutant strain does not replicate in minimal media with 2-ethyl hexyl sulfate as the sole sulfur source, in contrast to wild type or the complemented strain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the apo Rv3406 sulfatase at 2.5 A. The active site residues of Rv3406 and isoform AtsK from Pseudomonas putida are essentially superimposable
structure of AtsK in the apo form and in complexes with the cosubstrate 2-oxoglutarate, with 2-oxoglutarate and iron, and with 2-oxoglutarate, iron, and an alkyl sulfate ester. The overall fold of the enzyme is closely related to that of the taurine/2-oxoglutarate dioxygenase TauD and is similar to the fold observed for other members of the enzyme superfamily
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1.14.11.77 alkyl sulfatase
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