| EC |
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 |
| 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. 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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Ellis, A.J., Hales, S.G., Ur-Rehman, N.G. and White, G.F. Novel alkylsulfatases required for biodegradation of the branched primary alkyl sulfate surfactant 2-butyloctyl sulfate. Appl. Environ. Microbiol. 68 (2002) 31–36. [PMID: 11772605] |
| 2. |
Toesch, M., Schober, M. and Faber, K. Microbial alkyl- and aryl-sulfatases: mechanism, occurrence, screening and stereoselectivities. Appl. Microbiol. Biotechnol. 98 (2014) 1485–1496. [DOI] [PMID: 24352732] |
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| [EC 3.1.6.22 created 2021] |
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