Structural determinant of functionality in acyl lipid desaturases

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dc.citation.titleJournal of Lipid Research
dc.citation.volume59
dc.creatorSastre, Diego Emiliano
dc.creatorSaita, Emilio Adolfo
dc.creatorUttaro, Antonio Domingo
dc.creatorDe Mendoza, Diego
dc.creatorAltabe, Silvia Graciela
dc.date.accessioned2024-11-05T16:07:35Z
dc.date.available2024-11-05T16:07:35Z
dc.date.issued2018-10
dc.description.abstractLittle is known about the structure-function relationship of membrane-bound lipid desaturases. Using a domain-swapping strategy, we found that the N terminus (comprising the two first transmembrane segments) region of Bacillus cereus DesA desaturase improves Bacillus subtilis Des activity. In addition, the replacement of the first two transmembrane domains from Bacillus licheniformis inactive open reading frame (ORF) BL02692 with the corresponding domain from DesA was sufficient to resurrect this enzyme. Unexpectedly, we were able to restore the activity of ORF BL02692 with a single substitution (Cys40Tyr) of a cysteine localized in the first transmembrane domain close to the lipidwater interface. Substitution of eight residues (Gly90, Trp104, Lys172, His228, Pro257, Leu275, Tyr282, and Leu284) by site-directed mutagenesis produced inactive variants of DesA. Homology modeling of DesA revealed that His228 is part of the metal binding center, together with the canonical His boxes. Trp104 shapes the hydrophobic tunnel, whereas Gly90 and Lys172 are probably involved in substrate binding/recognition. Pro257, Leu275, Tyr282, and Leu284 might be relevant for the structural arrangement of the active site or interaction with electron donors. This study reveals the role of the N-terminal region of 5 phospholipid desaturases and the individual residues necessary for the activity of this class of enzymes.
dc.description.filFil: Sastre, Diego Emiliano. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario; Argentina.
dc.description.filFil: Saita, Emilio Adolfo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario; Argentina.
dc.description.filFil: Uttaro, Antonio Domingo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario; Argentina.
dc.description.filFil: De Mendoza, Diego. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario; Argentina.
dc.description.filFil: Altabe, Silvia Graciela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario; Argentina.
dc.description.sponsorshipFondo para la Investigación Científica y Tecnológica (FONCyT)
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica: PICT 2008
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET): P-UE 2016-IBR
dc.description.versionpeerreviewed
dc.format.extent1871-1879
dc.identifier.citationSastre, Diego Emiliano; Saita, Emilio Adolfo; Uttaro, Antonio Domingo; de Mendoza, Diego; Altabe, Silvia Graciela; Structural determinant of functionality in acyl lipid desaturases; Elsevier; Journal of Lipid Research Papers In Press; 59; 10; 10-2018; 1871-1879
dc.identifier.issn0022-2275
dc.identifier.urihttps://hdl.handle.net/2133/28049
dc.language.isoen
dc.publisherElsevier
dc.relation.publisherversionhttps://doi.org/10.1194/jlr.m085258
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S0022227520341791?via%3Dihub
dc.rightsopenAccess
dc.rights.holderSastre, Diego Emiliano
dc.rights.holderSaita, Emilio Adolfo
dc.rights.holderUttaro, Antonio Domingo
dc.rights.holderDe Mendoza, Diego
dc.rights.holderAltabe, Silvia Graciela
dc.rights.holderUniversidad Nacional de Rosario
dc.rights.textAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectBacillus
dc.subjectFatty acid desaturase
dc.subjectFatty acid biosynthesis
dc.subjectEnzyme mechanism
dc.subjectMembranes
dc.subjectProtein modeling
dc.titleStructural determinant of functionality in acyl lipid desaturases
dc.typearticulo
dc.type.versionpublishedVersion

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