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Literature summary extracted from

  • Aboulnaga, e.l.-.H.; Pinkenburg, O.; Schiffels, J.; El-Refai, A.; Buckel, W.; Selmer, T.
    Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli (2013), J. Bacteriol., 195, 3704-3713.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.3.8.1 synthesis expression of acetyl-coenzyme A C-acetyltransferase, 3-hydroxybutyryl-CoA dehydrogenase, crotonase, phosphate butyryltransferase, and butyrate kinase and the butyryl-CoA dehydrogenase complex composed of the dehydrogenase and two electron-transferring flavoprotein subunits as a single plasmid-encoded operon in Escherichia coli to confer butyrate-forming capability Clostridioides difficile

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.86 expressed in Escherichia coli Clostridioides difficile
1.3.1.109 expression in Escherichia coli Clostridioides difficile
1.3.8.1
-
 Clostridioides difficile
1.3.8.1 expressed in Escherichia coli Clostridioides difficile

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.86 0.002
-
 Ferredoxin pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 0.0025
-
 crotonyl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 0.01
-
 butyryl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 0.145
-
 NADH pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.109 0.01
-
 butanoyl-CoA pH 7.5, 22-25°C Clostridioides difficile
1.3.8.1 0.002
-
 reduced ferredoxin pH 7.5, 37°C Clostridioides difficile
1.3.8.1 0.0025
-
 crotonyl-CoA pH 7.5, 37°C Clostridioides difficile
1.3.8.1 0.0025
-
 crotonyl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.8.1 0.01
-
 butanoyl-CoA pH 7.5, 37°C Clostridioides difficile
1.3.8.1 0.01
-
 butyryl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.8.1 0.145
-
 NADH pH 7.5, 37°C Clostridioides difficile

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.86 110000
-
-
 Clostridioides difficile
1.3.8.1 110000
-
-
 Clostridioides difficile

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster Clostridioides difficile
-
 butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster Clostridioides difficile DSM 1296T
-
 butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.86 Clostridioides difficile
-
-
-
1.3.1.109 Clostridioides difficile Q18AQ1 and Q18AQ6 and Q18AQ5 Q18AQ1: Bcd2 protein, Q18AQ6: electron transfer flavoproteins subunit beta, Q18AQ5: electron transfer flavoprotein subunit alpha
-
1.3.1.109 Clostridioides difficile DSM 1296T Q18AQ1 and Q18AQ6 and Q18AQ5 Q18AQ1: Bcd2 protein, Q18AQ6: electron transfer flavoproteins subunit beta, Q18AQ5: electron transfer flavoprotein subunit alpha
-
1.3.8.1 Clostridioides difficile
-
-
-
1.3.8.1 Clostridioides difficile Q18AQ1
-
-
1.3.8.1 Clostridioides difficile DSM 1296
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.3.1.109 oxygen-stable Clostridioides difficile
1.3.8.1 enzyme is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air Clostridioides difficile

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.109
-
 Clostridioides difficile

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.86 crotonyl-CoA + NADH + ferredoxin
-
 Clostridioides difficile butyryl-CoA + ?
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 Clostridioides difficile butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 Clostridioides difficile DSM 1296T butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH Clostridioides difficile butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH Clostridioides difficile DSM 1296T butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 Clostridioides difficile (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 Clostridioides difficile DSM 1296T (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
-
 ?
1.3.8.1 butanoyl-CoA + FAD
-
 Clostridioides difficile 2-butenoyl-CoA + FADH2
-
 ?
1.3.8.1 butanoyl-CoA + FAD
-
 Clostridioides difficile DSM 1296 2-butenoyl-CoA + FADH2
-
 ?
1.3.8.1 crotonyl-CoA + electron transfer flavoprotein
-
 Clostridioides difficile butyryl-CoA + ?
-
 ?
1.3.8.1 crotonyl-CoA + O2 + 2 NADH + 2 H+ the crotonyl-CoA reduction mediated by the Clostridium difficile enzyme appears to be decoupled from ferredoxin reduction in the presence of air. Here, molecular oxygen apparently serves as an electron acceptor and hydrogen peroxide is formed as a second product Clostridioides difficile butanoyl-CoA + H2O2 + 2 NAD+
-
 ?
1.3.8.1 crotonyl-CoA + O2 + 2 NADH + 2 H+ the crotonyl-CoA reduction mediated by the Clostridium difficile enzyme appears to be decoupled from ferredoxin reduction in the presence of air. Here, molecular oxygen apparently serves as an electron acceptor and hydrogen peroxide is formed as a second product Clostridioides difficile DSM 1296 butanoyl-CoA + H2O2 + 2 NAD+
-
 ?
1.3.8.1 crotonyl-CoA + reduced ferredoxin
-
 Clostridioides difficile butanoyl-CoA + oxidized ferredoxin
-
 ?
1.3.8.1 crotonyl-CoA + reduced ferredoxin
-
 Clostridioides difficile DSM 1296 butanoyl-CoA + oxidized ferredoxin
-
 ?
1.3.8.1 additional information enzyme is a a bifurcating butyryl-CoA dehydrogenase which catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH. Since the reoxidation of ferredoxin by a membrane-bound ferredoxin:NAD+-oxidoreductase enables electron transport phosphorylation, additional ATP is formed. The butyryl-CoA dehydrogenase from Clostridium difficile is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air Clostridioides difficile ?
-
 ?
1.3.8.1 additional information enzyme is a a bifurcating butyryl-CoA dehydrogenase which catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH. Since the reoxidation of ferredoxin by a membrane-bound ferredoxin:NAD+-oxidoreductase enables electron transport phosphorylation, additional ATP is formed. The butyryl-CoA dehydrogenase from Clostridium difficile is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air Clostridioides difficile DSM 1296 ?
-
 ?
1.3.8.1 reduced ferredoxin + NAD+ + H+
-
 Clostridioides difficile oxidized ferredoxin + NADH
-
 ?
1.3.8.1 reduced ferredoxin + NAD+ + H+
-
 Clostridioides difficile DSM 1296 oxidized ferredoxin + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.109 trimer the butanoyl-CoA dehydrogenase complex is composed of the dehydrogenase and two electron-transferring flavoprotein subunits Clostridioides difficile

Synonyms

EC Number Synonyms Comment Organism
1.3.1.86 bcd2
-
 Clostridioides difficile
1.3.1.86 butyryl-CoA dehydrogenase complex
-
 Clostridioides difficile
1.3.1.86 CD1054
-
 Clostridioides difficile
1.3.1.109 bifurcating butyryl coenzyme A dehydrogenase/electron-transferring flavoprotein complex
-
 Clostridioides difficile
1.3.8.1 bcd2
-
 Clostridioides difficile
1.3.8.1 butyryl-CoA dehydrogenase complex
-
 Clostridioides difficile
1.3.8.1 CD1054
-
 Clostridioides difficile

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.1.109 23 25 assay at Clostridioides difficile

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.86 2 8 butyryl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 3 6 NADH pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 19
-
 crotonyl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 37
-
 Ferredoxin pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.109 2 8 butanoyl-CoA pH 7.5, 22-25°C Clostridioides difficile
1.3.8.1 2 8 butanoyl-CoA pH 7.5, 37°C Clostridioides difficile
1.3.8.1 2 8 butyryl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.8.1 3 6 NADH pH 7.5, 37°C Clostridioides difficile
1.3.8.1 19
-
 crotonyl-CoA pH 7.5, 37°C Clostridioides difficile
1.3.8.1 19
-
 crotonyl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.8.1 37
-
 reduced ferredoxin pH 7.5, 37°C Clostridioides difficile

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.86 7.5
-
 assay at Clostridioides difficile
1.3.1.109 7.5
-
 assay at Clostridioides difficile
1.3.8.1 7.5
-
 assay at Clostridioides difficile

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.86 FAD in the absence of ferredoxin, a remarkable stimulation of crotonyl-CoA reduction by FAD is observed Clostridioides difficile
1.3.1.86 Ferredoxin butyryl-CoA dehydrogenase from C. difficile belongs to the subfamily of bifurcating enzymes capable of coupling the exergonic reduction of crotonyl-CoA by NAD Hwith the endergonic reduction of ferredoxin by NADH Clostridioides difficile
1.3.1.86 NADH
-
 Clostridioides difficile
1.3.8.1 FAD in the absence of ferredoxin, a remarkable stimulation of crotonyl-CoA reduction by FAD is observed Clostridioides difficile
1.3.8.1 Ferredoxin butyryl-CoA dehydrogenase from Clostridium difficile belongs to the subfamily of bifurcating enzymes capable of coupling the exergonic reduction of crotonyl-CoA by NADH with the endergonic reduction of ferredoxin by NADH Clostridioides difficile
1.3.8.1 NAD+ enzyme is a a bifurcating butyryl-CoA dehydrogenase which catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH Clostridioides difficile
1.3.8.1 NADH
-
 Clostridioides difficile

General Information

EC Number General Information Comment Organism
1.3.1.86 metabolism butyryl-CoA dehydrogenase from C. difficile belongs to the subfamily of bifurcating enzymes capable of coupling the exergonic reduction of crotonyl-CoA by NAD Hwith the endergonic reduction of ferredoxin by NADH Clostridioides difficile
1.3.1.86 metabolism the genes necessary for butyrate formation from the genome of Clostridium difficile are expressed in Escherichia coli. The individual genes are assembled in a single plasmid vector into an artificial operon , which allows functional coexpression of the required genes and confers butyrate-forming capability to the host Clostridioides difficile
1.3.1.109 metabolism bifurcating butyryl-CoA dehydrogenase affects the energy yield of butyrate fermentation in the clostridial metabolism Clostridioides difficile
1.3.8.1 metabolism butyryl-CoA dehydrogenase from Clostridium difficile belongs to the subfamily of bifurcating enzymes capable of coupling the exergonic reduction of crotonyl-CoA by NADH with the endergonic reduction of ferredoxin by NADH Clostridioides difficile
1.3.8.1 metabolism the genes necessary for butyrate formation from the genome of Clostridium difficile are expressed in Escherichia coli. The individual genes are assembled in a single plasmid vector into an artificial operon , which allows functional coexpression of the required genes and confers butyrate-forming capability to the host Clostridioides difficile

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.1.86 250
-
 NADH pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 2800
-
 butyryl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 7600
-
 crotonyl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.86 18500
-
 Ferredoxin pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.1.109 2800
-
 butanoyl-CoA pH 7.5, 22-25°C Clostridioides difficile
1.3.8.1 250
-
 NADH pH 7.5, 37°C Clostridioides difficile
1.3.8.1 2800
-
 butanoyl-CoA pH 7.5, 37°C Clostridioides difficile
1.3.8.1 2800
-
 butyryl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.8.1 7600
-
 crotonyl-CoA pH 7.5, 37°C Clostridioides difficile
1.3.8.1 7600
-
 crotonyl-CoA pH 7.5, temperature not specified in the publication Clostridioides difficile
1.3.8.1 18500
-
 reduced ferredoxin pH 7.5, 37°C Clostridioides difficile