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Literature summary extracted from
- Studies of penicillin G acylase immobilization using highly porous cellulose-based polymeric membrane (2010), Appl. Biochem. Biotechnol., 160, 1130-1145.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.5.1.11 | additional information | penicillin G acylase immobilization using highly porous cellulose-based polymeric membrane, immobilized enzyme specific activity is 145 U/g, and a 2.4fold increase in activity compared to the free enzyme. The immobilized enzyme retains almost 50% activity after 107 days and 50 cycles of operation, method evaluation and enzyme stability, overview. Effect of different ionic molecules/compounds as ligands coupled to membrane on enzyme immobilization, best is Brilliant green | Escherichia coli |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.5.1.11 | crosslinking with glutaraldehyde fails to protect the immobilized enzyme activity in case of proline, tryptophan, and casein acid hydrolysate | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.11 | 19.5 | - |
penicillin G | pH 7.0, 40°C, free enzyme | Escherichia coli |  |
| 3.5.1.11 | 47.4 | - |
penicillin G | pH 7.0, 40°C, immobilized enzyme | Escherichia coli | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.5.1.11 | membrane | - |
Escherichia coli | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.11 | penicillin G + H2O | Escherichia coli | - |
phenylacetic acid + 6-aminopenicillanate | - |
? | |
| 3.5.1.11 | penicillin G + H2O | Escherichia coli NCIM 2400 | - |
phenylacetic acid + 6-aminopenicillanate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.11 | Escherichia coli | - |
- |
- |
| 3.5.1.11 | Escherichia coli NCIM 2400 | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.5.1.11 | proteolytic modification | processing of a single enzyme polypeptide precursor, which consists of a small alpha-subunit and a large beta-subunit, to form the heterodimer | 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 | phenylacetic acid + 6-aminopenicillanate | - |
? | |
| 3.5.1.11 | penicillin G + H2O | - |
Escherichia coli | phenylacetic acid + 6-aminopenicillanate | detection of product 6-aminopenicillanate by reaction with p-dimethylaminobenzaldehyde | ? | |
| 3.5.1.11 | penicillin G + H2O | - |
Escherichia coli NCIM 2400 | phenylacetic acid + 6-aminopenicillanate | - |
? | |
| 3.5.1.11 | penicillin G + H2O | - |
Escherichia coli NCIM 2400 | phenylacetic acid + 6-aminopenicillanate | detection of product 6-aminopenicillanate by reaction with p-dimethylaminobenzaldehyde | ? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.11 | heterodimer | the enzyme belongs to N-terminal nucleophile hydrolases that share a common fold around the active site bearing a catalytic serine, cysteine, or threonine at the N-terminal position | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.11 | penicillin G acylase | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.11 | 40 | - |
immobilized enzyme | Escherichia coli |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.11 | 20 | 50 | activity range of the free enzyme, profile overview | Escherichia coli |
| 3.5.1.11 | 20 | 60 | activity range of the immobilized enzyme, profile overview | Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.11 | 7.2 | - |
immobilized enzyme | Escherichia coli |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.11 | 3 | 10 | activity range of the immobilized enzyme, profile overview | Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.11 | physiological function | the enzyme is involved in synthesis of the anti-platelet agent and in enzymatic activation of pro-drugs in cancer therapy | Escherichia coli |
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