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A functional role identified for conserved charged residues at the active site entrance of lipoxygenase with double specificity
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- Alberti, Jean-Christophe (author)
- Univ Corse, Lab Biochim & Biol Mol Vegetales, CNRS SPE UMR6134, Campus Grimaldi,BP52, F-20250 Corte, France.;Univ Toulouse, INSA, UPS, INP,LISBP, 135 Ave Rangueil, F-31077 Toulouse, France.
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- Mariani, Magali (author)
- Univ Corse, Lab Biochim & Biol Mol Vegetales, CNRS SPE UMR6134, Campus Grimaldi,BP52, F-20250 Corte, France.
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- de Caraffa, Virginie Brunini-Bronzini (author)
- Univ Corse, Lab Biochim & Biol Mol Vegetales, CNRS SPE UMR6134, Campus Grimaldi,BP52, F-20250 Corte, France.
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- Univ Corse, Lab Biochim & Biol Mol Vegetales, CNRS SPE UMR6134, Campus Grimaldi,BP52, F-20250 Corte, France;Univ Toulouse, INSA, UPS, INP,LISBP, 135 Ave Rangueil, F-31077 Toulouse, France. Univ Corse, Lab Biochim & Biol Mol Vegetales, CNRS SPE UMR6134, Campus Grimaldi,BP52, F-20250 Corte, France. (creator_code:org_t)
- Elsevier BV, 2016
- 2016
- English.
- In: Journal of Molecular Catalysis B. - : Elsevier BV. - 1381-1177 .- 1873-3158. ; 123, s. 167-173
- Journal article (peer-reviewed)
Abstract
Subject headings
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- Plant lipoxygenases (LOXs) are a class of widespread dioxygenases catalyzing the hydroperoxidation of free polyunsaturated fatty acids, producing 9-hydroperoxides or 13-hydroperoxides from linoleic and alpha-linolenic acids, and are called 9-LOX or 13-LOX, respectively. Some LOXs produce both 9- and 13- hydroperoxides. The models proposed to explain the reaction mechanism specificity fail to explain the "double specificity" character of these LOXs. In this study, we used the olive LOX1 with double specificity to investigate the implication of the charged residues R265, R268, and K283 in the orientation of the substrate into the active site. These residues are present in a conserved pattern around the entrance of the active site. Our results show that these residues are involved in the penetration of the substrate into the active site: this positive patch could capture the carboxylate end of the substrate, and then guide it into the active site. Due to its position on alpha 2 helix, the residue K283 could have a more important role, its interaction with the substrate facilitating the motions of residues constituting the "cork of lipoxygenases" or the alpha 2 helix, by disrupting putative hydrogen and ionic bonds.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
Keyword
- Lipoxygenases
- Lipid peroxidation
- Mutagenesis
- Olea europaea L.
Publication and Content Type
- ref (subject category)
- art (subject category)
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