Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities-Reference-Cited by-同舟云学术

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Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities

Published:2017-07-07 Issue:15 Volume:284 Page:2442-2463
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Pégeot Henri¹,Mathiot Sandrine²,Perrot Thomas¹,Gense Frédéric²,Hecker Arnaud¹,Didierjean Claude²,Rouhier Nicolas¹

Affiliation:

1. UMR 1136 Interactions Arbres/Microorganismes; Faculté des Sciences et Technologies; Université de Lorraine/INRA; Vandoeuvre-lès-Nancy France

2. UMR 7036 CRM2, Equipe BioMod; Faculté des Sciences et Technologies; Université de Lorraine/CNRS; Vandoeuvre-lès-Nancy France

Funder

Agence Nationale de la Recherche

“Investissements d'Avenir” program

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.14138/fullpdf

Reference73 articles.

1. Structure, catalytic mechanism, and evolution of the glutathione transferases;Armstrong;Chem Res Toxicol,1997

2. The functions and regulation of glutathione S-transferases in plants;Marrs;Annu Rev Plant Physiol Plant Mol Biol,1996

3. Glutathione transferases in bacteria;Allocati;FEBS J,2009

4. Redox Regulation in Plants: Glutathione and “Redoxin” Related Families

5. Large-scale determination of sequence, structure, and function relationships in cytosolic glutathione transferases across the biosphere;Mashiyama;PLoS Biol,2014

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4. Repurposing Glutathione Transferases: Directed Evolution Combined with Chemical Modification for the Creation of a Semisynthetic Enzyme with High Hydroperoxidase Activity;Antioxidants;2023-12-25

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