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Literature summary for 3.5.1.11 extracted from

  • Xue, J.; Wang, A.; Zhou, C.; Shen, S.
    Penicillin acylase immobilization depending on macromolecular crowding and catalysis in aqueous-organic medium (2009), Bioprocess Biosyst. Eng., 32, 765-772.
    View publication on PubMed

Application

Application Comment Organism
synthesis penicillin acylase is one of the key pharmaceutical enzymes in the production of polysynthetic beta-lactam antibiotics Priestia megaterium

Protein Variants

Protein Variants Comment Organism
additional information immobilization of the enzyme on mesocellular silica foams from 0.1 M phosphate buffer, pH 7.0, the immobilized enzyme activity depends on molecular crowding and applied to catalysis in non-aqueous medium, addition of dextran, method optimization, using different enzyme preparations, organic solvents and mesocellular silica foams-dextran mixtures, overview Priestia megaterium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
penicillin G + H2O Priestia megaterium
-
phenylacetic acid + 6-aminopenicillanate
-
?

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation 1000 U/ml, 10 mg/ml Priestia megaterium
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
182
-
immobilized enzyme, pH 8.0, 37°C Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cephalosporin G + H2O
-
Priestia megaterium phenylacetic acid + 7-aminodeacetoxycephalosporanate
-
?
penicillin G + H2O
-
Priestia megaterium phenylacetic acid + 6-aminopenicillanate
-
?
penicillin G + H2O
-
Priestia megaterium phenylacetic acid + 6-aminopenicillanate detection by reaction with p-dimethyl-aminobenzaldehyde ?

Synonyms

Synonyms Comment Organism
penicillin acylase
-
Priestia megaterium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Priestia megaterium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Priestia megaterium

General Information

General Information Comment Organism
additional information The enzyme catalyzes the hydrolysis of the amidic bonds of penicillin G and cephalosporin G to produce key components in the synthesis of beta-lactam antibiotics Priestia megaterium