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Literature summary extracted from
- Multienzyme complexes of fatty acid oxidation from Escherichia coli K-12 and from a mutant with a defective L-3-hydroxyacyl coenzyme A dehydrogenase (1983), Biochim. Biophys. Acta, 750, 41-46.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.2.3 | Escherichia coli | - |
and mutant with a multienzyme complex with a defective L-3-hydroxyacyl-CoA dehydrogenase, EC 1.1.1.35, fadB64 | - |
| 5.3.3.3 | Escherichia coli | - |
- |
- |
| 5.3.3.3 | Escherichia coli | - |
strain fad B64 | - |
| 5.3.3.3 | Escherichia coli B / ATCC 11303 | - |
- |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.3.3.3 | 2.6 | - |
strain K-12YMel, substrate cis-3-octenoyl-CoA | Escherichia coli |
| 5.3.3.3 | 7.5 | - |
strain fad B64, substrate cis-3-octenoyl-CoA | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.2.3 | D-3-Hydroxydodecanoyl-CoA | - |
Escherichia coli | L-3-Hydroxydodecanoyl-CoA | - |
? |  |
| 5.1.2.3 | D-3-Hydroxydodecanoyl-CoA | - |
Escherichia coli B / ATCC 11303 | L-3-Hydroxydodecanoyl-CoA | - |
? | |
| 5.3.3.3 | cis-3-octenoyl-CoA | - |
Escherichia coli | ? | - |
? | |
| 5.3.3.3 | cis-3-octenoyl-CoA | - |
Escherichia coli B / ATCC 11303 | ? | - |
? | |
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