[Bacterial formate dehydrogenase. Substrate specificity and kinetic mechanism of S-formyl glutathione oxidation].
The substrate specificity of NAD-dependent formate dehydrogenase from the methylotrophic bacterium Achromobacter parvulus T1 was studied. The kinetic mechanism of S-formyl glutathione oxidation was determined. The initial velocity studies and inhibition analysis were carried out. It was shown that the kinetic mechanism for the enzyme with S-formyl glutathione as a substrate is similar to that with formate and is rapid-equilibrium random. Using independent methods, it was found that formate dehydrogenase forms a binary complex with S-formyl glutathione (Kd = 2.5 mM).
D000421:Alcaligenes / Q000201:enzymology*; D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D005560:Formate Dehydrogenases / Q000378:metabolism*; D005978:Glutathione / Q000031:analogs & derivatives* / Q000378:metabolism; D007700:Kinetics; D008433:Mathematics; D010084:Oxidation-Reduction; D013379:Substrate Specificity
C029468:S-formylglutathione; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; D005978:Glutathione
Bakterial'naia formiatdegidrogenaza. Substratnaia spetsifichnost' i kineticheskiĭ mekhanizm okisleniia S-formilglutationa.