Activating Compound | Comment | Organism | Structure |
---|---|---|---|
CN- | activates the enzyme in reaction with ferricytochrome c or ferricyanide as electron acceptors, but not with flavin D or FAd | Sus scrofa |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-chloromercuribenzoate | 0.1 mM, 40% inhibition | Bos taurus | |
4-chloromercuribenzoate | inhibition is reversible by glutathione | Sus scrofa | |
Hg2+ | - |
Sus scrofa | |
additional information | no inhibition by CN- | Sus scrofa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | 2 mol copper /mol FAD, cupric ion can be removed by dialysis against cyanide, copper is not involved in redox reaction | Bos taurus | |
Cu2+ | 10-12 copper ions per enzyme molecule, enzyme-bound copper. The Cu2+ does not play a role in the primary reduction of the flavin-bound enzyme | Sus scrofa |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
120000 | 220000 | gel filtration | Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
butanoyl-CoA + oxidized acceptor | Sus scrofa | - |
crotonyl-CoA + reduced acceptor | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Sus scrofa | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | - |
Sus scrofa | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
butanoyl-CoA + oxidized acceptor | - |
Sus scrofa | crotonyl-CoA + reduced acceptor | - |
r | |
additional information | no activity with octanoyl-CoA and acetyl-CoA | Sus scrofa | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
butyryl CoA dehydrogenase | - |
Sus scrofa |
butyryl coenzyme A dehydrogenase | - |
Sus scrofa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 38 | assay at | Sus scrofa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | about 5 or 6 FAD molecules per enzyme molecule | Bos taurus | |
FAD | enzyme-bound, flavin D | Sus scrofa | |
ferricytochrome c | - |
Sus scrofa | |
riboflavin | enzyme-bound | Sus scrofa |