Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases
| Autor: | Mathieu Schwartz, Simon R. Law, Elodie Sylvestre-Gonon, Nicolas Rouhier, Olivier Keech, Kevin Robe, Arnaud Hecker, Christian Dubos, Claude Didierjean |
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| Přispěvatelé: | Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Umea Plant Science Centre, Umeå University, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Equipe Nutrition Minérale et Stress Oxydatif (FEROS), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL), Rouhier, Nicolas |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
0301 basic medicine Review Plant Science phylogeny 01 natural sciences Serine chemistry.chemical_compound metabolic detoxification glutathione péroxydase chemistry.chemical_classification Vegetal Biology biology [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Chemistry glutathione transferases Biochemistry and Molecular Biology food and beverages [SDV.BV.BOT]Life Sciences [q-bio]/Vegetal Biology/Botanics [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Biochemistry Thioredoxin ligandin property Peroxidase xénobiotique lcsh:Plant culture cible herbicide 03 medical and health sciences photosynthetic organisms secondary metabolism structure xenobiotic detoxification lcsh:SB1-1110 xenobiotics [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] Secondary metabolism Botany Glutathione Botanik glutathion s transférase 030104 developmental biology Enzyme biology.protein détoxification métabolique Xenobiotic Biologie végétale Biokemi och molekylärbiologi 010606 plant biology & botany Cysteine |
| Zdroj: | Frontiers in Plant Science Frontiers in Plant Science, Frontiers, 2019, 10, pp.608. ⟨10.3389/fpls.2019.00608⟩ Frontiers in Plant Science, Vol 10 (2019) Frontiers in Plant Science (10), 608. (2019) |
| ISSN: | 1664-462X |
| DOI: | 10.3389/fpls.2019.00608⟩ |
| Popis: | Glutathione transferases (GSTs) belong to a ubiquitous multigenic family of enzymes involved in diverse biological processes including xenobiotic detoxification and secondary metabolism. A canonical GST is formed by two domains, the N-terminal one adopting a thioredoxin (TRX) fold and the C-terminal one an all-helical structure. The most recent genomic and phylogenetic analysis based on this domain organization allowed the classification of the GST family into 14 classes in terrestrial plants. These GSTs are further distinguished based on the presence of the ancestral cysteine (Cys-GSTs) present in TRX family proteins or on its substitution by a serine (Ser-GSTs). Cys-GSTs catalyze the reduction of dehydroascorbate and deglutathionylation reactions whereas Ser-GSTs catalyze glutathione conjugation reactions and eventually have peroxidase activity, both activities being important for stress tolerance or herbicide detoxification. Through non-catalytic, so-called ligandin properties, numerous plant GSTs also participate in the binding and transport of small heterocyclic ligands such as flavonoids including anthocyanins, and polyphenols. So far, this function has likely been underestimated compared to the other documented roles of GSTs. In this review, we compiled data concerning the known enzymatic and structural properties as well as the biochemical and physiological functions associated to plant GSTs having a conserved serine in their active site. |
| Databáze: | OpenAIRE |
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