Structural determinant of functionality in acyl lipid desaturases
dc.citation.title | Journal of Lipid Research | |
dc.citation.volume | 59 | |
dc.creator | Sastre, Diego Emiliano | |
dc.creator | Saita, Emilio Adolfo | |
dc.creator | Uttaro, Antonio Domingo | |
dc.creator | De Mendoza, Diego | |
dc.creator | Altabe, Silvia Graciela | |
dc.date.accessioned | 2024-11-05T16:07:35Z | |
dc.date.available | 2024-11-05T16:07:35Z | |
dc.date.issued | 2018-10 | |
dc.description.abstract | Little 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.fil | Fil: 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.fil | Fil: 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.fil | Fil: 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.fil | Fil: 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.fil | Fil: 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.sponsorship | Fondo para la Investigación Científica y Tecnológica (FONCyT) | |
dc.description.sponsorship | Agencia Nacional de Promoción Científica y Tecnológica: PICT 2008 | |
dc.description.sponsorship | Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET): P-UE 2016-IBR | |
dc.description.version | peerreviewed | |
dc.format.extent | 1871-1879 | |
dc.identifier.citation | Sastre, 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.issn | 0022-2275 | |
dc.identifier.uri | https://hdl.handle.net/2133/28049 | |
dc.language.iso | en | |
dc.publisher | Elsevier | |
dc.relation.publisherversion | https://doi.org/10.1194/jlr.m085258 | |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/pii/S0022227520341791?via%3Dihub | |
dc.rights | openAccess | |
dc.rights.holder | Sastre, Diego Emiliano | |
dc.rights.holder | Saita, Emilio Adolfo | |
dc.rights.holder | Uttaro, Antonio Domingo | |
dc.rights.holder | De Mendoza, Diego | |
dc.rights.holder | Altabe, Silvia Graciela | |
dc.rights.holder | Universidad Nacional de Rosario | |
dc.rights.text | Attribution 4.0 International | en |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.subject | Bacillus | |
dc.subject | Fatty acid desaturase | |
dc.subject | Fatty acid biosynthesis | |
dc.subject | Enzyme mechanism | |
dc.subject | Membranes | |
dc.subject | Protein modeling | |
dc.title | Structural determinant of functionality in acyl lipid desaturases | |
dc.type | articulo | |
dc.type.version | publishedVersion |
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