Protein disulfide isomerase and glutathione are alternative substrates in the one Cys catalytic cycle of glutathione peroxidase 7 - Bosello-Travain, Valentina; Conrad, Marcus; Cozza, Giorgio; Negro, Alessandro; Quartesan, Silvia; Rossetto, Monica; Roveri, Antonella; Toppo, Stefano; Ursini, Fulvio; Zaccarin, Mattia; Maiorino, Matilde (Biochimica et biophysica acta, 2013)
Keywords: Animals; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Catalysis; endoplasmic reticulum; enzyme substrates; glutathione; Glutathione - chemistry; Glutathione - genetics; Glutathione - metabolism; Glutathione peroxidase; Humans; Kinetics; Mice; Molecular Docking Simulation; molecular models; Mutation; oxidation; Oxidation-Reduction; Peroxidases - chemistry; Peroxidases - genetics; Peroxidases - metabolism; Peroxide; phospholipids; protein disulfide-isomerase; Protein Disulfide-Isomerases - chemistry; Protein Disulfide-Isomerases - genetics; Protein Disulfide-Isomerases - metabolism; protein-protein interactions; proteins; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Redox switch; Redoxin; substrate specificity; Substrate Specificity - genetics; surface plasmon resonance; GPxs; SecGPxs; GPx7; PCOOH; PDI; Peroxide; Trx; UP; GSH; TrxR; Glutathione peroxidase; GSSG; Prdxs; 2CysGPxs; 1CysGPx; Syn; CP; ER; CR; CysGPxs; ROOH; Sec; Redoxin; Redox switch; Kinetics