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Literature summary for 1.17.1.10 extracted from

  • Yamamoto, I.; Saiki, T.; Liu, S.M.; Ljungdahl, L.G.
    Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein (1983), J. Biol. Chem., 258, 1826-1832.
    View publication on PubMed

General Stability

General Stability Organism
azide stabilizes during purification Moorella thermoacetica
dithionite stabilizes during purification Moorella thermoacetica
glycerol stabilizes during purification Moorella thermoacetica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.109
-
formate
-
Moorella thermoacetica
0.117
-
NADP+
-
Moorella thermoacetica

Metals/Ions

Metals/Ions Comment Organism Structure
Iron 36 mol of iron per mol of enzyme Moorella thermoacetica
selenium 2 mol of selenium per mol of enzyme, resides in the alpha-subunit Moorella thermoacetica
Tungsten 2 mol of tungsten per mol of enzyme Moorella thermoacetica
Tungsten may exist as tungsten cofactor Moorella thermoacetica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
76000
-
alpha2 beta2, 2 * 96000 + 2 * 76000 SDS-PAGE Moorella thermoacetica
96000
-
alpha2 beta2, 2 * 96000 + 2 * 76000 SDS-PAGE Moorella thermoacetica
340000
-
gel filtration Moorella thermoacetica

Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
-
-
-

Oxidation Stability

Oxidation Stability Organism
extremely oxygen-sensitive Moorella thermoacetica

Purification (Commentary)

Purification (Comment) Organism
-
Moorella thermoacetica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1050
-
-
Moorella thermoacetica

Storage Stability

Storage Stability Organism
4°C, anaerobic conditions, glycerol, ammonium sulfate, 45 days, 35% loss of activity Moorella thermoacetica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO2 + NADPH enzyme also catalyzes: 1. reversible electron transfer between methyl viologen and NADPH, 2. reduction of FMN or FAD with NADPH (caused by a contaminating protein) Moorella thermoacetica formate + NADP+
-
?
CO2 + NADPH reduction of FMN or FAD with NADPH caused by a contaminating protein Moorella thermoacetica formate + NADP+
-
?

Subunits

Subunits Comment Organism
tetramer alpha2 beta2, 2 * 96000 + 2 * 76000 SDS-PAGE Moorella thermoacetica

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Moorella thermoacetica
NADPH
-
Moorella thermoacetica