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Literature summary for 3.5.1.11 extracted from
- Effects of catalytic site mutations on active expression of phage fused penicillin acylase (2010), J. Biotechnol., 145, 139-142.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme might be useful in the preparation of a wide range of semi-synthetic beta-lactam antibiotics from acyl side-chain precursors and beta-lactam nucleus | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in a phage display in Escherichia coli strain TG1 | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | directed evolution of penicillin acylase using phage display technology for extending its specificity. Fusion of the penicillin acylase to fd phage coat protein III and used pIII secretion signal sequence instead of penicillin acylase, which couples gene and enzyme on phage particle and can is useful for directed evolution of penicillin acylase. Penicillin acylase is functionally displayed on phage surface. Determination by site-directed mutagenesis of the effect of Ser B1 and Asn B241 variants on post-translational maturation of phage fused penicillin acylase, overview | Escherichia coli |
| N241G | site-directed mutagensis of subunit B residue, leads to reduced activity compared to the wild-type enzyme | Escherichia coli |
| N241S | site-directed mutagensis of subunit B residue, leads to reduced activity compared to the wild-type enzyme | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00614 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C, mutant N241G | Escherichia coli |  |
| 0.0102 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C, mutant N241S | Escherichia coli | |
| 0.03 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 23000 | - |
1 * 23000 + 1 * 62000, alphabeta, SDS-PAGE | Escherichia coli |
| 62000 | - |
1 * 23000 + 1 * 62000, alphabeta, SDS-PAGE | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
strain Migula 1895, ATCC 11105 | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | penicillin G acylase is a 86-kDa heterodimeric protein produced by intein-mediated auto-splicing of a 92-kDa precursor | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-nitro-5-[(phenyl-acetyl)amino]benzoic acid + H2O | - |
Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | 1 * 23000 + 1 * 62000, alphabeta, SDS-PAGE | Escherichia coli |
| More | penicillin G acylase is a 86-kDa heterodimeric protein produced by intein-mediated auto-splicing of a 92-kDa precursor | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| penicillin acylase | - |
Escherichia coli |
| penicillin G acylase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.204 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C, mutant N241S | Escherichia coli | |
| 0.354 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C, mutant N241G | Escherichia coli | |
| 15 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C, wild-type enzyme | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 20 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C, mutant N241S | Escherichia coli | |
| 57.6 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C, mutant N241G | Escherichia coli | |
| 500 | - |
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid | pH 7.0, 25°C | Escherichia coli | |
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