A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic
Linoleate dioxygenase-cytochrome P450 (DOX-CYP) fusion enzymes are common in pathogenic fungi. The DOX domains form hydroperoxy metabolites of 18:2n-6, which can be transformed by the CYP domains to 1,2- or 1,4-diols, epoxy alcohols, or to allene oxides. We have characterized two novel allene oxide...
| Autores: | , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2016 |
| País: | España |
| Institución: | Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| Repositorio: | Recercat. Dipósit de la Recerca de Catalunya |
| OAI Identifier: | oai:recercat.cat:2445/125188 |
| Acceso en línea: | https://hdl.handle.net/2445/125188 |
| Access Level: | acceso abierto |
| Palabra clave: | Metabolisme dels lípids Enzims Dioxines Proteïnes Fongs patògens Lipid metabolism Enzymes Dioxins Proteins Pathogenic fungi |
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A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. triticOliw, Ernst H.Aragó Belenguer, MarcChen, YangJernerén, FredrikMetabolisme dels lípidsEnzimsDioxinesProteïnesFongs patògensLipid metabolismEnzymesDioxinsProteinsPathogenic fungiLinoleate dioxygenase-cytochrome P450 (DOX-CYP) fusion enzymes are common in pathogenic fungi. The DOX domains form hydroperoxy metabolites of 18:2n-6, which can be transformed by the CYP domains to 1,2- or 1,4-diols, epoxy alcohols, or to allene oxides. We have characterized two novel allene oxide synthases (AOSs), namely, recombinant 8R-DOX-AOS of Coccidioides immitis (causing valley fever) and 8S-DOX-AOS of Zymoseptoria tritici (causing septoria tritici blotch of wheat). The 8R-DOX-AOS oxidized 18:2n-6 sequentially to 8R-hydroperoxy-9Z,12Z-octadecadienoic acid (8R-HPODE) and to an allene oxide, 8R(9)-epoxy-9,12Z-octadecadienoic acid, as judged from the accumulation of the α-ketol, 8S-hydroxy-9-oxo-12Z-octadecenoic acid. The 8S-DOX-AOS of Z. tritici transformed 18:2n-6 sequentially to 8S-HPODE and to an α-ketol, 8R-hydroxy-9-oxo-12Z-octadecenoic acid, likely formed by hydrolysis of 8S(9)-epoxy-9,12Z-octadecadienoic acid. The 8S-DOX-AOS oxidized [8R-2H]18:2n-6 to 8S-HPODE with retention of the 2H-label, suggesting suprafacial hydrogen abstraction and oxygenation in contrast to 8R-DOX-AOS. Both enzymes oxidized 18:1n-9 and 18:3n-3 to α-ketols, but the catalysis of the 8R- and 8S-AOS domains differed. 8R-DOX-AOS transformed 9R-HPODE to epoxy alcohols, but 8S-DOX-AOS converted 9S-HPODE to an α-ketol (9-hydroxy-10-oxo-12Z-octadecenoic acid) and epoxy alcohols in a ratio of ∼1:2. Whereas all fatty acid allene oxides described so far have a conjugated diene impinging on the epoxide, the allene oxides formed by 8-DOX-AOS are unconjugated.American Society for Biochemistry and Molecular Biology2018201820162018info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion11 p.application/pdfhttps://hdl.handle.net/2445/125188Articles publicats en revistes (Ciències Fisiològiques)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.1194/jlr.M068981Journal of Lipid Research, 2016, vol. 57, num. 8, p. 1518-1528https://doi.org/10.1194/jlr.M068981(c) American Society for Biochemistry and Molecular Biology, 2016info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1251882026-05-29T05:05:01Z |
| dc.title.none.fl_str_mv |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic |
| title |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic |
| spellingShingle |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic Oliw, Ernst H. Metabolisme dels lípids Enzims Dioxines Proteïnes Fongs patògens Lipid metabolism Enzymes Dioxins Proteins Pathogenic fungi |
| title_short |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic |
| title_full |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic |
| title_fullStr |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic |
| title_full_unstemmed |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic |
| title_sort |
A new class of fatty acid allene oxide formed by the DOX-P450 fusion proteins of human and plant pathogenic fungi, C. immitis and Z. tritic |
| dc.creator.none.fl_str_mv |
Oliw, Ernst H. Aragó Belenguer, Marc Chen, Yang Jernerén, Fredrik |
| author |
Oliw, Ernst H. |
| author_facet |
Oliw, Ernst H. Aragó Belenguer, Marc Chen, Yang Jernerén, Fredrik |
| author_role |
author |
| author2 |
Aragó Belenguer, Marc Chen, Yang Jernerén, Fredrik |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
Metabolisme dels lípids Enzims Dioxines Proteïnes Fongs patògens Lipid metabolism Enzymes Dioxins Proteins Pathogenic fungi |
| topic |
Metabolisme dels lípids Enzims Dioxines Proteïnes Fongs patògens Lipid metabolism Enzymes Dioxins Proteins Pathogenic fungi |
| description |
Linoleate dioxygenase-cytochrome P450 (DOX-CYP) fusion enzymes are common in pathogenic fungi. The DOX domains form hydroperoxy metabolites of 18:2n-6, which can be transformed by the CYP domains to 1,2- or 1,4-diols, epoxy alcohols, or to allene oxides. We have characterized two novel allene oxide synthases (AOSs), namely, recombinant 8R-DOX-AOS of Coccidioides immitis (causing valley fever) and 8S-DOX-AOS of Zymoseptoria tritici (causing septoria tritici blotch of wheat). The 8R-DOX-AOS oxidized 18:2n-6 sequentially to 8R-hydroperoxy-9Z,12Z-octadecadienoic acid (8R-HPODE) and to an allene oxide, 8R(9)-epoxy-9,12Z-octadecadienoic acid, as judged from the accumulation of the α-ketol, 8S-hydroxy-9-oxo-12Z-octadecenoic acid. The 8S-DOX-AOS of Z. tritici transformed 18:2n-6 sequentially to 8S-HPODE and to an α-ketol, 8R-hydroxy-9-oxo-12Z-octadecenoic acid, likely formed by hydrolysis of 8S(9)-epoxy-9,12Z-octadecadienoic acid. The 8S-DOX-AOS oxidized [8R-2H]18:2n-6 to 8S-HPODE with retention of the 2H-label, suggesting suprafacial hydrogen abstraction and oxygenation in contrast to 8R-DOX-AOS. Both enzymes oxidized 18:1n-9 and 18:3n-3 to α-ketols, but the catalysis of the 8R- and 8S-AOS domains differed. 8R-DOX-AOS transformed 9R-HPODE to epoxy alcohols, but 8S-DOX-AOS converted 9S-HPODE to an α-ketol (9-hydroxy-10-oxo-12Z-octadecenoic acid) and epoxy alcohols in a ratio of ∼1:2. Whereas all fatty acid allene oxides described so far have a conjugated diene impinging on the epoxide, the allene oxides formed by 8-DOX-AOS are unconjugated. |
| publishDate |
2016 |
| dc.date.none.fl_str_mv |
2016 2018 2018 2018 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
https://hdl.handle.net/2445/125188 |
| url |
https://hdl.handle.net/2445/125188 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
Reproducció del document publicat a: https://doi.org/10.1194/jlr.M068981 Journal of Lipid Research, 2016, vol. 57, num. 8, p. 1518-1528 https://doi.org/10.1194/jlr.M068981 |
| dc.rights.none.fl_str_mv |
(c) American Society for Biochemistry and Molecular Biology, 2016 info:eu-repo/semantics/openAccess |
| rights_invalid_str_mv |
(c) American Society for Biochemistry and Molecular Biology, 2016 |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
11 p. application/pdf |
| dc.publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
| publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
| dc.source.none.fl_str_mv |
Articles publicats en revistes (Ciències Fisiològiques) reponame:Recercat. Dipósit de la Recerca de Catalunya instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| instname_str |
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| reponame_str |
Recercat. Dipósit de la Recerca de Catalunya |
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Recercat. Dipósit de la Recerca de Catalunya |
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1869403172890476544 |
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15,812455 |