2019
DOI: 10.1074/jbc.ra119.008439
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Oleate hydratase from Staphylococcus aureus protects against palmitoleic acid, the major antimicrobial fatty acid produced by mammalian skin

Abstract: Edited by Dennis R. Voelker Oleate hydratases (OhyAs) belong to a large family of bacterial proteins catalyzing the hydration or isomerization of double bonds in unsaturated fatty acids. A Staphylococcus aureus gene (Sa0102) is predicted to encode an OhyA. Here, we recombinantly expressed and purified SaOhyA and found that it forms a homodimer that requires FAD for activity. SaOhyA hydrates only unsaturated fatty acids containing cis-9 double bonds, but not fatty acids with trans-9 double bonds or cis double b… Show more

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Cited by 44 publications
(56 citation statements)
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“…The kinetics of RpOhy showed a significant cooperative effect, which has rarely been reported for Ohys. Only recently for Staphylococcus aureus Ohy, similar cooperative kinetics was reported with a similar Hill coefficient of 2.2 ± 0.3 (Subramanian et al 2019). Most Ohys have been reported to display regular Michaelis-Menten kinetics with K M in the range from 0.1 to 0.6 mM and V max from 0.6 to 4 U/mg (Bevers et al 2009;Volkov et al 2010;Rosberg-Cody et al 2011;Joo et al 2012a;Kim et al 2012;Joo et al 2012b).…”
Section: Rpohy Is a Novel Oleate Hydratasesupporting
confidence: 54%
“…The kinetics of RpOhy showed a significant cooperative effect, which has rarely been reported for Ohys. Only recently for Staphylococcus aureus Ohy, similar cooperative kinetics was reported with a similar Hill coefficient of 2.2 ± 0.3 (Subramanian et al 2019). Most Ohys have been reported to display regular Michaelis-Menten kinetics with K M in the range from 0.1 to 0.6 mM and V max from 0.6 to 4 U/mg (Bevers et al 2009;Volkov et al 2010;Rosberg-Cody et al 2011;Joo et al 2012a;Kim et al 2012;Joo et al 2012b).…”
Section: Rpohy Is a Novel Oleate Hydratasesupporting
confidence: 54%
“…Each S. aureus fakB sequence was cloned into plasmid pCS119, which has a pCM28 backbone (31), no ribosomal binding site, and uses a sarA P1 promoter to drive expression. DNA sequences for S. pneumoniae strain TIGR4 fakB1 (SP_1557), fakB2 (SP_1112), and fakB3 (SP_0742) genes did not contain a ribosomal binding site or a His 6 tag and were cloned into pET28a (Novagen), to add an N-terminal His 6 tag, and ligated into pPJ480 (32), which is a pCS119 plasmid derivative containing the sarA P1 promoter as well as a ribosomal binding site. Restriction followed by ligation reactions were used to insert the fakB gene of interest into either pCS119 (S. aureus expression) or pPJ480 (S. pneumoniae expression).…”
Section: Bacterial Strainsmentioning
confidence: 99%
“…However, efflux pumps FarE ( 20 ) and Tet38 ( 21 ) prevent the cellular accumulation of AFAs, which are still able to bind to S. aureus . Additionally, this bacterium possesses a functional oleate hydratase, which hydrates and thereby detoxifies AFAs containing cis -9 double bonds ( 22 ).…”
Section: Introductionmentioning
confidence: 99%
“…However, efflux pumps FarE (20) and Tet38 (21) prevent the cellular accumulation of AFAs, which are still able to bind to S. aureus. Additionally, this bacterium possesses a functional oleate hydratase, which hydrates and thereby detoxifies AFAs containing cis-9 double bonds (22). Strikingly, S. aureus grown for a few hours in the presence of subinhibitory amounts of AFAs survives subsequent exposures to otherwise bactericidal AFA concentrations (20,23), suggesting that the bacteria activate an AFA stress response program.…”
mentioning
confidence: 99%