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Literature summary for 3.5.1.11 extracted from
- Properties of penicillin amidase immobilized by copolymerization with acrylamide (1979), Biotechnol. Bioeng., 21, 1543-1552.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| phenylacetic acid | competitive inhibition | Escherichia coli |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.2 | - |
benzylpenicillin | - |
Escherichia coli | |
| 0.8 | - |
benzylpenicillin | immobilized enzyme | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| penicillin G + H2O | - |
Escherichia coli | 6-aminopenicillanate + phenylacetic acid | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
higher thermal stability of immobilized enzyme | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7.6 | - |
Escherichia coli |
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