Steady-state kinetic studies of glutathione reductase.
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.
Serafini
M T
MT
Departamento de Ingeniería Química y Bioquímica, Universidad de Barcelona, Tarragona, Spain.
Romeu
A
A
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
D005656:Fungal Proteins; D009249:NADP; D005980:Glutathione Reductase; D005978:Glutathione