2014
DOI: 10.1002/pro.2528
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Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase

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 b-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 alkylsul… Show more

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Cited by 8 publications
(6 citation statements)
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“…The third group includes enzymes with the metallo-β-lactamase-like domain in the N-terminus and SCP-2-like domain in C-terminus. Six sulfatases with different substrate specificities have been characterized to date: SdsA, YraS, and YjcS with activity toward sodium dodecyl sulfate (SDS) ( Davison et al, 1992 ; Liang et al, 2014 ; Navais et al, 2014 ), SdsAP and SdsA1 with activity toward primary sulfate esters including sodium dodecyl sulfate ( Hagelueken et al, 2006 ; Long et al, 2011 ; Schober et al, 2011 ) and Pisa1 with activity toward secondary alkyl sulfates ( Schober et al, 2011 ). Enzymes from this group differ in the mechanism of action and could cleave either S-O or C-O bond causing the retention or inversion of the product alcohol, which could be verified using chiral or labeled substrates.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…The third group includes enzymes with the metallo-β-lactamase-like domain in the N-terminus and SCP-2-like domain in C-terminus. Six sulfatases with different substrate specificities have been characterized to date: SdsA, YraS, and YjcS with activity toward sodium dodecyl sulfate (SDS) ( Davison et al, 1992 ; Liang et al, 2014 ; Navais et al, 2014 ), SdsAP and SdsA1 with activity toward primary sulfate esters including sodium dodecyl sulfate ( Hagelueken et al, 2006 ; Long et al, 2011 ; Schober et al, 2011 ) and Pisa1 with activity toward secondary alkyl sulfates ( Schober et al, 2011 ). Enzymes from this group differ in the mechanism of action and could cleave either S-O or C-O bond causing the retention or inversion of the product alcohol, which could be verified using chiral or labeled substrates.…”
Section: Introductionmentioning
confidence: 99%
“…However, they are mainly focused on the phylogenetic identification of the isolates and the alkylsulfatase activity testing using Native Page Zymography without the detailed enzyme characteristics. Therefore, there are only five well-characterized alkylsulfatases with known sequence and confirmed activity toward SDS ( Davison et al, 1992 ; Hagelueken et al, 2006 ; Long et al, 2011 ; Liang et al, 2014 ; Navais et al, 2014 ). This year a first attempt to identify the enzymes involved in the further SDS metabolic pathway in P. aeruginosa PAO1 was performed.…”
Section: Introductionmentioning
confidence: 99%
“…The second gene, yjcS (EcSMS35_1714 in E. coli ), is an alkyl-sulfatase. This enzyme has been first described in Pseudomonas spp ., where a strain carrying this enzyme was able to grow on the surfactant sodium dodecyl sulphate (SDS), and the gene has been characterised in E. coli as well 30,31 .…”
Section: Resultsmentioning
confidence: 99%
“…Alkylsulfatase activity was measured by the rate of phenol red oxidation at 557 nm ( ε 557 = 44,100 M −1 cm −1 ) (Liang et al 2014 ). The measurements were made in 96-well plates, and the absorbance decrease was read on a Spark 10 M tablet spectrophotometer (Tecan, Switzerland).…”
Section: Methodsmentioning
confidence: 99%