Literature DB >> 6615926

[Bacterial formate dehydrogenase. Substrate specificity and kinetic mechanism of S-formyl glutathione oxidation].

V I Tishkov, A M Egorov, V O Popov.   

Abstract

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).

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Year:  1983        PMID: 6615926

Source DB:  PubMed          Journal:  Biokhimiia        ISSN: 0320-9725


  3 in total

1.  The kinetic mechanism of formate dehydrogenase from bakery yeast.

Authors:  A E Serov; A S Popova; V I Tishkov
Journal:  Dokl Biochem Biophys       Date:  2002 Jan-Feb       Impact factor: 0.788

2.  Effect of pH on kinetic parameters of NAD+-dependent formate dehydrogenase.

Authors:  A V Mesentsev; V S Lamzin; V I Tishkov; T B Ustinnikova; V O Popov
Journal:  Biochem J       Date:  1997-01-15       Impact factor: 3.857

Review 3.  NAD(+)-dependent formate dehydrogenase.

Authors:  V O Popov; V S Lamzin
Journal:  Biochem J       Date:  1994-08-01       Impact factor: 3.857

  3 in total

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