Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Wang, S.; Huang, H.; Kahnt, H.; Mueller, A.; Köpke, M.; Thauer, R.
    NADP-specific electron-bifurcating [FeFe]-hydrogenase in a functional complex with formate dehydrogenase in Clostridium autoethanogenum grown on CO (2013), J. Bacteriol., 195, 4373-4386.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.B29 additional information
-
 additional information Km value of NADH is below 0.5 mM, of NADPH is above 1 mM Clostridium autoethanogenum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.B29 cytoplasm enzyme complex comprises 6% of the cytoplasmic proteins Clostridium autoethanogenum 5737
-

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.B29 Clostridium autoethanogenum S5Z061 and S5YUC5 S5Z061: [FeFe]-hydrogenase subunit HytA, S5YUC5: formate dehydrogenase subunit FdhA
-
1.2.1.B29 Clostridium autoethanogenum DSM 10061 S5Z061 and S5YUC5 S5Z061: [FeFe]-hydrogenase subunit HytA, S5YUC5: formate dehydrogenase subunit FdhA
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.2.1.B29 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)

EC Number Purification (Comment) Organism
1.2.1.B29
-
 Clostridium autoethanogenum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.B29 7
-
 formate formation reaction, pH 7.5, 37°C Clostridium autoethanogenum
1.2.1.B29 8.7
-
 H2 formation reaction, pH 7.5, 37°C Clostridium autoethanogenum
1.2.1.B29 13
-
 substrate H2, pH 6.5, 37°C Clostridium autoethanogenum
1.2.1.B29 15.2
-
 substrate formate, pH 7.5, 37°C Clostridium autoethanogenum
1.2.1.B29 26.5
-
 H2 formation reaction, pH 6.0, 37°C Clostridium autoethanogenum
1.2.1.B29 29.2
-
 substrate H2, pH 7.5, 37°C Clostridium autoethanogenum
1.2.1.B29 32
-
 substrate H2, pH 6.5, 37°C Clostridium autoethanogenum
1.2.1.B29 35
-
 formate formation, substrates CO2 and H2, pH 7.5, 37°C Clostridium autoethanogenum
1.2.1.B29 41
-
 formate formation, substrates CO2 and H2, pH 7.0, 37°C Clostridium autoethanogenum
1.2.1.B29 18000
-
 substrates H2 and methyl viologen, pH 7.5, 37°C Clostridium autoethanogenum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.B29 2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum 2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum DSM 10061 2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum 2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum DSM 10061 2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum 2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum DSM 10061 2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum DSM 10061 NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 r
1.2.1.B29 H2 + NADP+ + 2 oxidized methyl viologen
-
 Clostridium autoethanogenum ? + NADPH + H+ + 2 reduced methyl viologen
-
 r
1.2.1.B29 H2 + NADP+ + 2 oxidized methyl viologen
-
 Clostridium autoethanogenum DSM 10061 ? + NADPH + H+ + 2 reduced methyl viologen
-
 r
1.2.1.B29 NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
 Clostridium autoethanogenum H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 r

Subunits

EC Number Subunits Comment Organism
1.2.1.B29 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

Synonyms

EC Number Synonyms Comment Organism
1.2.1.B29 electron-bifurcating [FeFe]-hydrogenase
-
 Clostridium autoethanogenum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.B29 37
-
 assay at Clostridium autoethanogenum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.B29 6
-
 H2 formation from formate Clostridium autoethanogenum
1.2.1.B29 6
-
 H2 formation from NADPH and reduced ferredoxin Clostridium autoethanogenum
1.2.1.B29 6.5
-
 NADP and ferredoxin reduction with H2 Clostridium autoethanogenum
1.2.1.B29 7
-
 CO2 reduction with H2 to formate Clostridium autoethanogenum
1.2.1.B29 7.5
-
 NADP and ferredoxin reduction with formate at pH 7.5 Clostridium autoethanogenum

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.B29 NADH Km value is above 1 mM, NADPH is preferred over NADH Clostridium autoethanogenum
1.2.1.B29 NADPH Km value is below 0.5 mM, NADPH is preferred over NADH Clostridium autoethanogenum

General Information

EC Number General Information Comment Organism
1.2.1.B29 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