BRENDA - Enzyme Database show
show all sequences of 1.2.1.B29

NADP-specific electron-bifurcating [FeFe]-hydrogenase in a functional complex with formate dehydrogenase in Clostridium autoethanogenum grown on CO

Wang, S.; Huang, H.; Kahnt, H.; Mueller, A.; Köpke, M.; Thauer, R.; J. Bacteriol. 195, 4373-4386 (2013)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Km value of NADH is below 0.5 mM, of NADPH is above 1 mM
Clostridium autoethanogenum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
enzyme complex comprises 6% of the cytoplasmic proteins
Clostridium autoethanogenum
5737
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium autoethanogenum
S5Z061 and S5YUC5
S5Z061: [FeFe]-hydrogenase subunit HytA, S5YUC5: formate dehydrogenase subunit FdhA
-
Clostridium autoethanogenum DSM 10061
S5Z061 and S5YUC5
S5Z061: [FeFe]-hydrogenase subunit HytA, S5YUC5: formate dehydrogenase subunit FdhA
-
Oxidation Stability
Oxidation Stability
Organism
the enzyme is rapidly inactivated in the presence of only trace amounts of O2, and it loses activity upon dilution to much below 1 mg/ml even under strictly anoxic conditions
Clostridium autoethanogenum
Purification (Commentary)
Commentary
Organism
-
Clostridium autoethanogenum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7
-
formate formation reaction, pH 7.5, 37°C
Clostridium autoethanogenum
8.7
-
H2 formation reaction, pH 7.5, 37°C
Clostridium autoethanogenum
13
-
substrate H2, pH 6.5, 37°C
Clostridium autoethanogenum
15.2
-
substrate formate, pH 7.5, 37°C
Clostridium autoethanogenum
26.5
-
H2 formation reaction, pH 6.0, 37°C
Clostridium autoethanogenum
29.2
-
substrate H2, pH 7.5, 37°C
Clostridium autoethanogenum
32
-
substrate H2, pH 6.5, 37°C
Clostridium autoethanogenum
35
-
formate formation, substrates CO2 and H2, pH 7.5, 37°C
Clostridium autoethanogenum
41
-
formate formation, substrates CO2 and H2, pH 7.0, 37°C
Clostridium autoethanogenum
18000
-
substrates H2 and methyl viologen, pH 7.5, 37°C
Clostridium autoethanogenum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
r
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
H2 + NADP+ + 2 oxidized methyl viologen
-
734087
Clostridium autoethanogenum
? + NADPH + H+ + 2 reduced methyl viologen
-
-
-
r
H2 + NADP+ + 2 oxidized methyl viologen
-
734087
Clostridium autoethanogenum DSM 10061
? + NADPH + H+ + 2 reduced methyl viologen
-
-
-
r
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
purified complex is composed of seven different subunits. The 78.8-kDa subunit FdhA is a selenocysteine- and tungsten-containing formate dehydrogenase, the 65.5-kDa subunit HytB is an ironsulfur flavin mononucleotide protein harboring the NADP binding site, the 51.4-kDa subunit HytA is the [FeFe]-hydrogenase, and the 18.1-kDa HytC, 28.6-kDa HytD, 19.9-kDa HytE1, and 20.1-kDa HytE2 subunits are iron-sulfur proteins
Clostridium autoethanogenum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Clostridium autoethanogenum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
H2 formation from formate; H2 formation from NADPH and reduced ferredoxin
Clostridium autoethanogenum
6.5
-
NADP and ferredoxin reduction with H2
Clostridium autoethanogenum
7
-
CO2 reduction with H2 to formate
Clostridium autoethanogenum
7.5
-
NADP and ferredoxin reduction with formate at pH 7.5
Clostridium autoethanogenum
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
Km value is above 1 mM, NADPH is preferred over NADH
Clostridium autoethanogenum
NADPH
Km value is below 0.5 mM, NADPH is preferred over NADH
Clostridium autoethanogenum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
Km value is above 1 mM, NADPH is preferred over NADH
Clostridium autoethanogenum
NADPH
Km value is below 0.5 mM, NADPH is preferred over NADH
Clostridium autoethanogenum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Km value of NADH is below 0.5 mM, of NADPH is above 1 mM
Clostridium autoethanogenum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
enzyme complex comprises 6% of the cytoplasmic proteins
Clostridium autoethanogenum
5737
-
Oxidation Stability (protein specific)
Oxidation Stability
Organism
the enzyme is rapidly inactivated in the presence of only trace amounts of O2, and it loses activity upon dilution to much below 1 mg/ml even under strictly anoxic conditions
Clostridium autoethanogenum
Purification (Commentary) (protein specific)
Commentary
Organism
-
Clostridium autoethanogenum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7
-
formate formation reaction, pH 7.5, 37°C
Clostridium autoethanogenum
8.7
-
H2 formation reaction, pH 7.5, 37°C
Clostridium autoethanogenum
13
-
substrate H2, pH 6.5, 37°C
Clostridium autoethanogenum
15.2
-
substrate formate, pH 7.5, 37°C
Clostridium autoethanogenum
26.5
-
H2 formation reaction, pH 6.0, 37°C
Clostridium autoethanogenum
29.2
-
substrate H2, pH 7.5, 37°C
Clostridium autoethanogenum
32
-
substrate H2, pH 6.5, 37°C
Clostridium autoethanogenum
35
-
formate formation, substrates CO2 and H2, pH 7.5, 37°C
Clostridium autoethanogenum
41
-
formate formation, substrates CO2 and H2, pH 7.0, 37°C
Clostridium autoethanogenum
18000
-
substrates H2 and methyl viologen, pH 7.5, 37°C
Clostridium autoethanogenum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
r
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum DSM 10061
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
r
H2 + NADP+ + 2 oxidized methyl viologen
-
734087
Clostridium autoethanogenum
? + NADPH + H+ + 2 reduced methyl viologen
-
-
-
r
H2 + NADP+ + 2 oxidized methyl viologen
-
734087
Clostridium autoethanogenum DSM 10061
? + NADPH + H+ + 2 reduced methyl viologen
-
-
-
r
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
734087
Clostridium autoethanogenum
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
purified complex is composed of seven different subunits. The 78.8-kDa subunit FdhA is a selenocysteine- and tungsten-containing formate dehydrogenase, the 65.5-kDa subunit HytB is an ironsulfur flavin mononucleotide protein harboring the NADP binding site, the 51.4-kDa subunit HytA is the [FeFe]-hydrogenase, and the 18.1-kDa HytC, 28.6-kDa HytD, 19.9-kDa HytE1, and 20.1-kDa HytE2 subunits are iron-sulfur proteins
Clostridium autoethanogenum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Clostridium autoethanogenum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
H2 formation from formate; H2 formation from NADPH and reduced ferredoxin
Clostridium autoethanogenum
6.5
-
NADP and ferredoxin reduction with H2
Clostridium autoethanogenum
7
-
CO2 reduction with H2 to formate
Clostridium autoethanogenum
7.5
-
NADP and ferredoxin reduction with formate at pH 7.5
Clostridium autoethanogenum
General Information
General Information
Commentary
Organism
physiological function
the enzyme complex catalyzes both the reversible coupled reduction of ferredoxin and NADP+ with H2 or formate and the reversible formation of H2 and CO2 from formate. The complex has two functions in vivo, namely, to normally catalyze CO2 reduction to formate with NADPH and reduced ferredoxin in the Wood-Ljungdahl pathway and to catalyze H2 formation from NADPH and reduced ferredoxin when these redox mediators get too reduced during unbalanced growth on CO
Clostridium autoethanogenum
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme complex catalyzes both the reversible coupled reduction of ferredoxin and NADP+ with H2 or formate and the reversible formation of H2 and CO2 from formate. The complex has two functions in vivo, namely, to normally catalyze CO2 reduction to formate with NADPH and reduced ferredoxin in the Wood-Ljungdahl pathway and to catalyze H2 formation from NADPH and reduced ferredoxin when these redox mediators get too reduced during unbalanced growth on CO
Clostridium autoethanogenum
Other publictions for EC 1.2.1.B29
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734087
Wang
NADP-specific electron-bifurca ...
Clostridium autoethanogenum, Clostridium autoethanogenum DSM 10061
J. Bacteriol.
195
4373-4386
2013
-
-
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1
1
-
-
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-
5
1
-
1
-
-
-
10
-
11
1
1
-
-
-
4
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
1
1
-
-
-
-
1
-
1
-
-
10
-
11
1
1
-
-
-
4
-
-
-
-
1
1
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