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Literature summary for 3.5.1.11 extracted from
- Glycosylation and pH stability of penicillin G acylase from Providencia rettgeri produced in Pichia pastoris (2009), Arch. Biol. Sci., 61, 581-586.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| industry | PAC is used in industrial synthesis of semi-synthetic antibiotics | Providencia rettgeri |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Providencia pastoris strain LN5.5 with secretion to the culture medium | Providencia rettgeri |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 24500 | - |
1 * 24500, alpha-subunit, + 1 * 65000, beta-subunit, SDS-PAGE, the subunits are held together by noncovalent forces | Providencia rettgeri |
| 65000 | - |
1 * 24500, alpha-subunit, + 1 * 65000, beta-subunit, SDS-PAGE, the subunits are held together by noncovalent forces | Providencia rettgeri |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| penicillin G + H2O | Providencia rettgeri | - |
6-aminopenicillanic acid + phenyl acetic acid | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Providencia rettgeri | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | both subunits alpha and beta of the enzyme are N-glycosylated, while the beta-subunit also contains O-glycans , determination of the glycosylation pattern of recombinant enzyme expressed in Pichia pastoris, overview | Providencia rettgeri |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Providencia pastoris strain LN5.5 by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography | Providencia rettgeri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| penicillin G + H2O | - |
Providencia rettgeri | 6-aminopenicillanic acid + phenyl acetic acid | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | 1 * 24500, alpha-subunit, + 1 * 65000, beta-subunit, SDS-PAGE, the subunits are held together by noncovalent forces | Providencia rettgeri |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAC | - |
Providencia rettgeri |
| penicillin G acylase | - |
Providencia rettgeri |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Providencia rettgeri |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Providencia rettgeri |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme catalyzes the conversion of benzylpenicillin, via hydrolysis of the acyl group in the benzylpenicillin side chain, to release phenylacetic acid and 6-aminopenicillanic acid | Providencia rettgeri |
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