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Structural and functional analysis show that the Escherichia coli uncharacterized protein Y jc S is likely an alkylsulfatase
Author(s) -
Liang Yajing,
Gao Zengqiang,
Dong Yuhui,
Liu Quansheng
Publication year - 2014
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2528
Subject(s) - escherichia coli , chemistry , food science , biochemistry , gene
Abstract Sodium dodecyl sulfate (SDS) is a widely used anionic surfactant in industry and research settings, and is known to have a detrimental effect to the environment. The pathway of SDS degradation by bacteria is initiated by an alkylsulfatase and the oxidized product, 1‐dodecanoic acid, subsequently enters into the β‐oxidation pathway and is used as a carbon source. In this work, we solved the crystal structure of Escherichia coli uncharacterized protein YjcS and identified that it belongs to the Type III alkylsulfatase with a signal peptide (residues 1–29) at the N terminus. YjcS hydrolyzed SDS and the double mutant D184N‐H185A located in the conserved HXHXDH catalytic motif abolished this activity.