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Literature summary for 5.4.99.5 extracted from
- Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities (1976), Eur. J. Biochem., 71, 327-336.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40000 | - |
x * 40000, chorismate mutase/prephenate dehydratase, tryptic fingerprinting suggests that the 40000 MW subunits are closely similar if not identical | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
K12 | - |
| Escherichia coli | - |
bifunctional enzyme chorismate mutase/prephenate dehydratase | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Chorismate | - |
Escherichia coli | Prephenate | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000, chorismate mutase/prephenate dehydratase, tryptic fingerprinting suggests that the 40000 MW subunits are closely similar if not identical | Escherichia coli |
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Release 2023.1 (January 2023)
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