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Literature summary for 3.5.1.11 extracted from

  • Miranda, V.; Wilson, L.; Cardenas, C.; Illanes, A.
    Reactivation of immobilized penicillin G acylase: Influence of cosolvents and catalytic modulators (2011), J. Mol. Catal. B, 68, 77-82.
No PubMed abstract available
Search for more literature for 3.5.1.11

Inhibitors

Inhibitors Comment Organism Structure
2-thienylacetic acid competitive inhibitor Escherichia coli
6-aminopenicillanic acid non-competitive inhibitor Escherichia coli
7-amino-3-desacetoxycephalosporanic acid non-competitive inhibitor Escherichia coli
phenylacetic acid competitive inhibitor Escherichia coli

Organic Solvent Stability

Organic Solvent Comment Organism
dioxane investigation of inactivation of immobilized enzyme by 70% (v/v) dioxan Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
commercial preparation Escherichia coli

Renatured (Commentary)

Renatured (Comment) Organism
partially inactivated immobilized enzyme, by addition of e.g. ethyleneglycol and catalytic modulators (competitive (reduction in reactivation yield) and non-competitive (increase in reactivation yield) inhibitors) Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
penicillin G + H2O
-
 Escherichia coli phenylacetic acid + 6-aminopenicillanate
-
 ?

Synonyms

Synonyms Comment Organism
penicillin G acylase
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5
-
 stable during the whole working period Escherichia coli