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Literature summary extracted from

  • Senerovic, L.; Stankovic, N.; Ljubijanic, G.; Vasiljevic, B.
    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

EC Number Application Comment Organism
3.5.1.11 industry PAC is used in industrial synthesis of semi-synthetic antibiotics Providencia rettgeri

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.11 expression in Providencia pastoris strain LN5.5 with secretion to the culture medium Providencia rettgeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.11 24500
-
 1 * 24500, alpha-subunit, + 1 * 65000, beta-subunit, SDS-PAGE, the subunits are held together by noncovalent forces Providencia rettgeri
3.5.1.11 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.11 penicillin G + H2O Providencia rettgeri
-
 6-aminopenicillanic acid + phenyl acetic acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.11 Providencia rettgeri
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.11 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)

EC Number Purification (Comment) Organism
3.5.1.11 recombinant enzyme from Providencia pastoris strain LN5.5 by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography Providencia rettgeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.11 penicillin G + H2O
-
 Providencia rettgeri 6-aminopenicillanic acid + phenyl acetic acid
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.11 heterodimer 1 * 24500, alpha-subunit, + 1 * 65000, beta-subunit, SDS-PAGE, the subunits are held together by noncovalent forces Providencia rettgeri

Synonyms

EC Number Synonyms Comment Organism
3.5.1.11 PAC
-
 Providencia rettgeri
3.5.1.11 penicillin G acylase
-
 Providencia rettgeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.11 25
-
 assay at Providencia rettgeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.11 6
-
 assay at Providencia rettgeri

General Information

EC Number General Information Comment Organism
3.5.1.11 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