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EC 3.1.6.22 Details

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EC number

3.1.6.22

Accepted name

branched primary-alkylsulfatase

Reaction

2-butyloctyl sulfate + H₂O = 2-butyloctan-1-ol + sulfate

Other name(s)

DP1 (gene name), type III branched primary-alkylsulfatase

Systematic name

branched primary-alkyl sulfate ester sulfohydrolase

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 family. The enzyme, characterized from a Pseudomonas strain, is specific for branched primary-alkyl sulfate esters and does not act on linear substrates such as dodecyl sulfate. cf. EC 3.1.6.1, arylsulfatase (type I), EC 1.14.11.77, alkyl sulfatase, EC 3.1.6.19, (R)-specific secondary-alkylsulfatase (type III) and EC 3.1.6.21, linear primary-alkylsulfatase.

History

created 2021

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.2 With a heme protein as acceptor

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.6 With a nitrogenous group as acceptor

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.99 With unknown physiological acceptors

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.98.1. undefined

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

3.1 Acting on ester bonds

3.1.1 Carboxylic-ester hydrolases

3.1.2 Thioester hydrolases

3.1.3 Phosphoric-monoester hydrolases

3.1.4 Phosphoric-diester hydrolases

3.1.5 Triphosphoric-monoester hydrolases

3.1.6 Sulfuric-ester hydrolases

3.1.6.1 arylsulfatase (type I)

3.1.6.2 steryl-sulfatase

3.1.6.3 glycosulfatase

3.1.6.4 N-acetylgalactosamine-6-sulfatase

3.1.6.5 created 1961, deleted 1964

3.1.6.6 choline-sulfatase

3.1.6.7 cellulose-polysulfatase

3.1.6.8 cerebroside-sulfatase

3.1.6.9 chondro-4-sulfatase

3.1.6.10 chondro-6-sulfatase

3.1.6.11 disulfoglucosamine-6-sulfatase

3.1.6.12 N-acetylgalactosamine-4-sulfatase

3.1.6.13 iduronate-2-sulfatase

3.1.6.14 N-acetylglucosamine-6-sulfatase

3.1.6.15 N-sulfoglucosamine-3-sulfatase

3.1.6.16 monomethyl-sulfatase

3.1.6.17 D-lactate-2-sulfatase

3.1.6.18 glucuronate-2-sulfatase

3.1.6.19 (R)-specific secondary-alkylsulfatase (type III)

3.1.6.20 S-sulfosulfanyl-L-cysteine sulfohydrolase

3.1.6.21 linear primary-alkylsulfatase

3.1.6.22 branched primary-alkylsulfatase

3.1.7 Diphosphoric-monoester hydrolases

3.1.8 Phosphoric-triester hydrolases

3.1.11 Exodeoxyribonucleases producing 5′-phosphomonoesters

3.1.12 Exodeoxyribonucleases producing 3′-phosphomonoesters

3.1.13 Exoribonucleases producing 5′-phosphomonoesters

3.1.14 Exoribonucleases producing 3'-phosphomonoesters

3.1.15 Exonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters

3.1.16 Exonucleases that are active with either ribo- or deoxyribonucleic acids and produce 3'-phosphomonoesters

3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters

3.1.22 Endodeoxyribonucleases producing 3'-phosphomonoesters

3.1.23 Site-specific endodeoxyribonucleases: cleavage is sequence specific (deleted sub-subclass)

3.1.24 Site specific endodeoxyribonucleases: cleavage is not sequence specific (deleted sub-subclass)

3.1.25 Site-specific endodeoxyribonucleases that are specific for altered bases

3.1.26 Endoribonucleases producing 5'-phosphomonoesters

3.1.27 Endoribonucleases producing 3'-phosphomonoesters

3.1.30 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters

3.1.31 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 3'-phosphomonoesters

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)