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Literature summary for 1.17.1.9 extracted from

  • Ruschig, U.; Mueller, U.; Willnow, P.; Hoepner, T.
    CO2 Reduction to formate by NADH catalysed by formate dehydrogenase from Pseudomonas oxalaticus (1976), Eur. J. Biochem., 70, 325-330.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 formate
-
 Cupriavidus oxalaticus
40
-
 CO2
-
 Cupriavidus oxalaticus

Organism

Organism UniProt Comment Textmining
Cupriavidus oxalaticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formate + NAD+ enzyme catalyzes formate oxidation about 30times faster than the CO2 reduction Cupriavidus oxalaticus CO2 + NADH + H+
-
 r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Cupriavidus oxalaticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
 CO2 reduction Cupriavidus oxalaticus
7.4
-
 formate oxidation Cupriavidus oxalaticus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Cupriavidus oxalaticus