BRENDA - Enzyme Database show

A reversible electron-bifurcating ferredoxin- and NAD-dependent [FeFe]-hydrogenase (HydABC) in Moorella thermoacetica

Wang, S.; Huang, H.; Kahnt, J.; Thauer, R.K.; J. Bacteriol. 195, 1267-1275 (2013)

Data extracted from this reference:

KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.12.1.4
additional information
-
H2
apparent Km value for H2 is about 6% in the gas phase, pH 7.5, 45°C
Moorella thermoacetica
1.12.1.4
0.2
-
NAD+
pH 7.5, 45°C
Moorella thermoacetica
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.12.1.4
Iron
purified enzyme contains 31 irons and 0.8 FMN per heterotrimer
Moorella thermoacetica
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.12.1.4
17000
-
-
Moorella thermoacetica
1.12.1.4
63000
-
-
Moorella thermoacetica
1.12.1.4
67000
-
-
Moorella thermoacetica
1.12.1.4
300000
-
gel filtration
Moorella thermoacetica
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.12.1.4
Moorella thermoacetica
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.12.1.4
under strictly anoxic conditions, the enzyme is inactivated in the presence of even trace amounts of O2
Moorella thermoacetica
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.12.1.4
4.6
-
oxidation of ferredoxin, pH 7.5, 45°C
Moorella thermoacetica
1.12.1.4
57.5
-
reduction of ferredoxin, pH 7.5, 45°C
Moorella thermoacetica
1.12.1.4
195
-
reduction of methyl viologen, pH 7.5, 45°C
Moorella thermoacetica
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.12.1.4
NAD+ + 2 oxidized ferredoxin + 2 H2
-
740618
Moorella thermoacetica
NADH + 3 H+ + 2 reduced ferredoxin
ferredoxin reduction with H2 is driven by the exergonic reduction of NAD+ (E0 -320 mV) with H2. In the absence of NAD+, ferredoxin is not reduced
-
-
?
1.12.1.4
NAD+ + 2 oxidized methyl viologen + 2 H2
-
740618
Moorella thermoacetica
NADH + 3 H+ + 2 reduced methyl viologen
-
-
-
?
1.12.1.4
NADH + 3 H+ + 2 reduced ferredoxin
-
740618
Moorella thermoacetica
NAD+ + 2 oxidized ferredoxin + 2 H2
per mol NADH, about 2 mol H2 is formed
-
-
?
1.12.1.4
NADH + 3 H+ + 2 reduced methyl viologen
-
740618
Moorella thermoacetica
NAD+ + 2 oxidized methyl viologen + 2 H2
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.12.1.4
heterohexamer
2 * 67000, subunit HydB, plus 2 * 63000, subunit HydA, plus 2 * 17000, subunit HydC, SDS-PAGE
Moorella thermoacetica
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.12.1.4
FMN
purified enzyme contains 31 irons and 0.8 FMN per heterotrimer
Moorella thermoacetica
1.12.1.4
iron-sulfur centre
subunit HydA (63 kDa) is predicted to harbor the H cluster, i.e., the [6Fe4S] hydrogenase active site, three [4Fe4S] clusters, and one [2Fe2S] cluster. Subunit HydB (67 kDa) is predicted to harbor three [4Fe4S] clusters, a flavin binding site, and an NAD binding site. HydC (17 kDa) is predicted to harbor one [2Fe2S] cluster
Moorella thermoacetica
1.12.1.4
NAD+
-
Moorella thermoacetica
1.12.1.4
NADH
-
Moorella thermoacetica
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.12.1.4
FMN
purified enzyme contains 31 irons and 0.8 FMN per heterotrimer
Moorella thermoacetica
1.12.1.4
iron-sulfur centre
subunit HydA (63 kDa) is predicted to harbor the H cluster, i.e., the [6Fe4S] hydrogenase active site, three [4Fe4S] clusters, and one [2Fe2S] cluster. Subunit HydB (67 kDa) is predicted to harbor three [4Fe4S] clusters, a flavin binding site, and an NAD binding site. HydC (17 kDa) is predicted to harbor one [2Fe2S] cluster
Moorella thermoacetica
1.12.1.4
NAD+
-
Moorella thermoacetica
1.12.1.4
NADH
-
Moorella thermoacetica
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.12.1.4
additional information
-
H2
apparent Km value for H2 is about 6% in the gas phase, pH 7.5, 45°C
Moorella thermoacetica
1.12.1.4
0.2
-
NAD+
pH 7.5, 45°C
Moorella thermoacetica
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.12.1.4
Iron
purified enzyme contains 31 irons and 0.8 FMN per heterotrimer
Moorella thermoacetica
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.12.1.4
17000
-
-
Moorella thermoacetica
1.12.1.4
63000
-
-
Moorella thermoacetica
1.12.1.4
67000
-
-
Moorella thermoacetica
1.12.1.4
300000
-
gel filtration
Moorella thermoacetica
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.12.1.4
under strictly anoxic conditions, the enzyme is inactivated in the presence of even trace amounts of O2
Moorella thermoacetica
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.12.1.4
4.6
-
oxidation of ferredoxin, pH 7.5, 45°C
Moorella thermoacetica
1.12.1.4
57.5
-
reduction of ferredoxin, pH 7.5, 45°C
Moorella thermoacetica
1.12.1.4
195
-
reduction of methyl viologen, pH 7.5, 45°C
Moorella thermoacetica
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.12.1.4
NAD+ + 2 oxidized ferredoxin + 2 H2
-
740618
Moorella thermoacetica
NADH + 3 H+ + 2 reduced ferredoxin
ferredoxin reduction with H2 is driven by the exergonic reduction of NAD+ (E0 -320 mV) with H2. In the absence of NAD+, ferredoxin is not reduced
-
-
?
1.12.1.4
NAD+ + 2 oxidized methyl viologen + 2 H2
-
740618
Moorella thermoacetica
NADH + 3 H+ + 2 reduced methyl viologen
-
-
-
?
1.12.1.4
NADH + 3 H+ + 2 reduced ferredoxin
-
740618
Moorella thermoacetica
NAD+ + 2 oxidized ferredoxin + 2 H2
per mol NADH, about 2 mol H2 is formed
-
-
?
1.12.1.4
NADH + 3 H+ + 2 reduced methyl viologen
-
740618
Moorella thermoacetica
NAD+ + 2 oxidized methyl viologen + 2 H2
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.12.1.4
heterohexamer
2 * 67000, subunit HydB, plus 2 * 63000, subunit HydA, plus 2 * 17000, subunit HydC, SDS-PAGE
Moorella thermoacetica