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Literature summary for 1.17.1.9 extracted from

  • Tishkov, V.I.; Galkin, A.G.; Marchenko, G.N.; Egorova, O.A.; Sheluho, D.V.; Kulakova, L.B.; Dementieva, L.A.; Egorov, A.M.
    Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacements (1993), Biochem. Biophys. Res. Commun., 192, 976-981.
    View publication on PubMed
Search for more literature for 1.17.1.9

Cloned(Commentary)

Cloned (Comment) Organism
wild-type enzyme and mutant enzymes C255S and C255M, expression in Escherichia coli Pseudomonas sp.

Protein Variants

Protein Variants Comment Organism
C255M high resistance to inactivation by Hg2+, increase of enzyme stability at 25°C, decrease of thermostability above 45°C. Native enzyme preserves more than 80% of initial activity after 2 h in 7 M urea. The mutant enzyme is completely inactive Pseudomonas sp.
C255S high resistance to inactivation by Hg2+, increase of enzyme stability at 25°C, decrease of thermostability above 45°C. Native enzyme preserves more than 80% of initial activity after 2 h in 7 M urea. The mutant enzyme is completely inactive Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 NAD+ wild-type enzyme Pseudomonas sp.
0.3
-
 NAD+ mutant enzyme C255S Pseudomonas sp.
0.6
-
 NAD+ mutant enzyme C255M Pseudomonas sp.
7.5
-
 formate wild-type enzyme and mutant enzyme C255S Pseudomonas sp.
20
-
 formate mutant enzyme C255M Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formate + NAD+
-
 Pseudomonas sp. CO2 + NADH + H+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Pseudomonas sp.