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Literature summary for 3.5.1.11 extracted from
- The effect of ultrasound as a new method of studying conformational transitions in enzyme active sites. pH- and temperature-induced conformational transitions in the active centre of penicillin amidase (1975), FEBS Lett., 49, 325-328.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0031 | - |
benzylpenicillin | - |
Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| penicillin G + H2O | - |
Escherichia coli | 6-aminopenicillanate + phenylacetic acid | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.15 | - |
- |
Escherichia coli |
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Release 2023.1 (January 2023)
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