Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Tishkov, V.I.; Matorin, A.D.; Rojkova, A.M.; Fedorchuk, V.V.; Savitsky, P.A.; Dementieva, L.A.; Lamzin, V.S.; Mezentzev, A.V.; Popov, V.O.
    Site-directed mutagenesis of the formate dehydrogenase active center: role of the His332-Gln313 pair in enzyme catalysis (1996), FEBS Lett., 390, 104-108.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.17.1.9 H332F complete loss of activity. The mutant is still able to bind coenzyme, but not substrate or analogues Pseudomonas sp.
1.17.1.9 Q313E mutation shifts the pK of the group controlling formate binding from less than 5.5 in wild-type enzyme to 7.6 Pseudomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.1.9 N3-
-
 Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.1.9 0.07
-
 NAD+ wild-type enzyme and mutant enzyme Q313E Pseudomonas sp.
1.17.1.9 4
-
 formate mutant enzyme Q313E Pseudomonas sp.
1.17.1.9 7
-
 formate wild-type enzyme Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.9 Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.9 NAD+
-
 Pseudomonas sp.