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Literature summary for 1.11.1.18 extracted from
- Thermostability of the vanadium bromoperoxidase from Corallina officinalis (1993), Biochem. Soc. Trans., 21, 445S.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corallina officinalis | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.47 | - |
- |
Corallina officinalis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione | i.e. monochlorodimedone | Corallina officinalis | ? | - |
? |  |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
the oligomeric structure of the enzyme is not apparently disrupted by exposure to 60°C. The purified bromoperoxidase at 135 nM is maintained in the absence of any protective reagent at 60°C for 24 h. Within 30 min about 60% of the original activity is lost but no further decline in activity is seen over the full course of the incubation | Corallina officinalis |
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