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Literature summary extracted from
- Cloning and sequencing of the coenzyme B(12)-binding domain of isobutyryl-CoA mutase from Streptomyces cinnamonensis, reconstitution of mutase activity, and characterization of the recombinant enzyme produced in Escherichia coli (1999), J. Biol. Chem., 274, 31679-31685.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.4.99.13 | IcmB, expression in Escherichia coli, IcmB shows significant identity to several cobalamin-dependent proteins | Streptomyces virginiae |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.13 | 0.054 | - |
2-methylpropanoyl-CoA | pH 7.4, 30ºC | Streptomyces virginiae |  |
| 5.4.99.13 | 0.057 | - |
butanoyl-CoA | pH 7.4, 30ºC | Streptomyces virginiae | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.13 | 14300 | - |
alpha2beta2, IcmA2IcmB2, 2 * 62500 + 2 * 14300, gel filtration, IcmB provides the cobalamin-binding domain | Streptomyces virginiae |
| 5.4.99.13 | 62500 | - |
alpha2beta2, IcmA2IcmB2, 2 * 62500 + 2 * 14300, gel filtration, IcmB provides the cobalamin-binding domain | Streptomyces virginiae |
| 5.4.99.13 | 153000 | - |
gel filtration | Streptomyces virginiae |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.13 | 2-methylpropanoyl-CoA | Streptomyces virginiae | valine and fatty acid catabolism | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | Streptomyces virginiae | biosynthesis of the antibiotic monesin-A | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | Streptomyces virginiae A3823.5 | valine and fatty acid catabolism | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | Streptomyces virginiae A3823.5 | biosynthesis of the antibiotic monesin-A | butanoyl-CoA | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.13 | Streptomyces virginiae | Q9RJ84 | A3823.5 | - |
| 5.4.99.13 | Streptomyces virginiae A3823.5 | Q9RJ84 | A3823.5 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.4.99.13 | recombinant IcmB is purified using Q-Sepharose, and two Mono Q column chromatography | Streptomyces virginiae |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.4.99.13 | 2-methylpropanoyl-CoA = butanoyl-CoA | either a random or ordered sequential mechanism | Streptomyces virginiae |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.13 | 3.3 | - |
the specific activity varies with the molar ratio of IcmA to IcmB | Streptomyces virginiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.13 | 2-methylpropanoyl-CoA | - |
Streptomyces virginiae | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | valine and fatty acid catabolism | Streptomyces virginiae | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | biosynthesis of the antibiotic monesin-A | Streptomyces virginiae | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | - |
Streptomyces virginiae A3823.5 | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | valine and fatty acid catabolism | Streptomyces virginiae A3823.5 | butanoyl-CoA | - |
r | |
| 5.4.99.13 | 2-methylpropanoyl-CoA | biosynthesis of the antibiotic monesin-A | Streptomyces virginiae A3823.5 | butanoyl-CoA | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.13 | tetramer | alpha2beta2, IcmA2IcmB2, 2 * 62500 + 2 * 14300, gel filtration, IcmB provides the cobalamin-binding domain | Streptomyces virginiae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.13 | ICM | - |
Streptomyces virginiae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.13 | 30 | - |
the reaction is incubated at darkness | Streptomyces virginiae |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.13 | 38.2 | - |
butanoyl-CoA | pH 7.4, 30ºC | Streptomyces virginiae | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.13 | 7.4 | - |
the activity diminishes only slightly at pH 6 and 8 | Streptomyces virginiae |
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