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Literature summary extracted from
- Crotonobetaine reductase from Escherichia coli consists of two proteins (1999), Biochim. Biophys. Acta, 1431, 166-178.
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.3.8.13 | 41500 | - |
4 * 41500, SDS-PAGE | Escherichia coli |
| 1.3.8.13 | 164400 | - |
gel filtration | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.8.13 | Escherichia coli | P60584 | - |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.3.8.13 | 233 | - |
pH 7.5, 22°C | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.8.13 | crotonobetaine + reduced benzylviologen | - |
Escherichia coli | gamma-butyrobetaine + oxidized benzylviologen | - |
? |  |
| 1.3.8.13 | additional information | presence of L-carnitine dehydratase is required for enzymatic activity | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.3.8.13 | tetramer | 4 * 41500, SDS-PAGE | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.8.13 | caiA | - |
Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.8.13 | FAD | contains non-covalently bound FAD in a molar ratio of 1:1 | Escherichia coli | |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.3.8.13 | Escherichia coli | - |
- |
5.6 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.3.8.13 | physiological function | presence of L-carnitine dehydratase is required for enzymatic activity. In the crotonobetaine reductase reaction one dimer of L-carnitine dehydratase associates with one tetramer of crotonobetaine reductase. A further low-molecular-mass effector described for the L-carnitine dehydratase is also necessary for crotonobetaine reductase activity | Escherichia coli |
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Release 2023.1 (January 2023)
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