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Literature summary for 1.3.8.1 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

Application Comment Organism
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)

Cloned (Comment) Organism
-
Clostridioides difficile
expressed in Escherichia coli Clostridioides difficile

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
-
Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile
-
-
-
Clostridioides difficile Q18AQ1
-
-
Clostridioides difficile DSM 1296
-
-
-

Oxidation Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butanoyl-CoA + FAD
-
Clostridioides difficile 2-butenoyl-CoA + FADH2
-
?
butanoyl-CoA + FAD
-
Clostridioides difficile DSM 1296 2-butenoyl-CoA + FADH2
-
?
crotonyl-CoA + electron transfer flavoprotein
-
Clostridioides difficile butyryl-CoA + ?
-
?
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+
-
?
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+
-
?
crotonyl-CoA + reduced ferredoxin
-
Clostridioides difficile butanoyl-CoA + oxidized ferredoxin
-
?
crotonyl-CoA + reduced ferredoxin
-
Clostridioides difficile DSM 1296 butanoyl-CoA + oxidized ferredoxin
-
?
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 ?
-
?
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 ?
-
?
reduced ferredoxin + NAD+ + H+
-
Clostridioides difficile oxidized ferredoxin + NADH
-
?
reduced ferredoxin + NAD+ + H+
-
Clostridioides difficile DSM 1296 oxidized ferredoxin + NADH
-
?

Synonyms

Synonyms Comment Organism
bcd2
-
Clostridioides difficile
butyryl-CoA dehydrogenase complex
-
Clostridioides difficile
CD1054
-
Clostridioides difficile

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Clostridioides difficile

Cofactor

Cofactor Comment Organism Structure
FAD in the absence of ferredoxin, a remarkable stimulation of crotonyl-CoA reduction by FAD is observed Clostridioides difficile
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
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
NADH
-
Clostridioides difficile

General Information

General Information Comment Organism
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
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]

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