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Literature summary 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]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.11 | 0.0031 | - |
benzylpenicillin | - |
Escherichia coli |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.11 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.11 | - |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.11 | penicillin G + H2O | - |
Escherichia coli | 6-aminopenicillanate + phenylacetic acid | - |
? | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.11 | 8.15 | - |
- |
Escherichia coli |
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Release 2023.1 (January 2023)
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