title: Steady-state kinetic studies of glutathione reductase.
abstract: The steady-state kinetic studies of yeast glutathione reductase, performed when [GSSG] = 10[NADPH] in the assay mixture, show that at concentrations of GSSG under 450 microM the enzymatic mechanism pathway is ping-pong. Furthermore, in the case of higher values, the enzymatic kinetics follows a sequential pathway. However when the glutathione reductase reaction passes to the ping-pong mechanism, the inhibition effect by excess of NADPH is stronger than when the reaction takes place over the sequential mechanism.
authors.affiliation: Departamento de Ingeniería Química y Bioquímica, Universidad de Barcelona, Tarragona, Spain.
authors.forename: M T
authors.initials: MT
authors.lastname: Serafini
authors.forename: A
authors.initials: A
authors.lastname: Romeu
mesh_terms: D005656:Fungal Proteins / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D005980:Glutathione Reductase / Q000378:metabolism*; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology
chemical_list: D005656:Fungal Proteins; D009249:NADP; D005980:Glutathione Reductase; D005978:Glutathione