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 (Comment) | Organism |
---|---|
- |
Clostridioides difficile |
expressed in Escherichia coli | Clostridioides difficile |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
110000 | - |
- |
Clostridioides difficile |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridioides difficile | - |
- |
- |
Clostridioides difficile | Q18AQ1 | - |
- |
Clostridioides difficile DSM 1296 | - |
- |
- |
Oxidation Stability | Organism |
---|---|
enzyme is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air | Clostridioides difficile |
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 | Comment | Organism |
---|---|---|
bcd2 | - |
Clostridioides difficile |
butyryl-CoA dehydrogenase complex | - |
Clostridioides difficile |
CD1054 | - |
Clostridioides difficile |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Clostridioides difficile |
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 | 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 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 |