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Literature summary for 1.17.1.9 extracted from

  • Hoepner, T.; Trautwein, A.
    Some properties of formate dehydrogenase (1972), Z. Naturforsch. B, 27, 1075-1076.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
formate activates in a slow reaction of which the velocity is dependent on the concentration of formate Cupriavidus oxalaticus

General Stability

General Stability Organism
inactivated by light irradiation Cupriavidus oxalaticus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe 5-8 mol of iron per mol of enzyme Cupriavidus oxalaticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
200000
-
enzyme form FDHI, sucrose density gradient centrifugation Cupriavidus oxalaticus
300000
-
enzyme form FDHII, sucrose density gradient centrifugation Cupriavidus oxalaticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
formate + NAD+ Cupriavidus oxalaticus enzyme provides NADH for synthesis CO2 + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Cupriavidus oxalaticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formate + NAD+
-
Cupriavidus oxalaticus CO2 + NADH + H+
-
?
formate + NAD+ enzyme provides NADH for synthesis Cupriavidus oxalaticus CO2 + NADH + H+
-
?
formate + phenazine methosulfate
-
Cupriavidus oxalaticus CO2 + reduced phenazine methosulfate
-
?

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.6
-
optimal stability Cupriavidus oxalaticus

Cofactor

Cofactor Comment Organism Structure
FMN enzyme contains at least 1 mol of FMN per mol of enzyme Cupriavidus oxalaticus
NAD+
-
Cupriavidus oxalaticus