Not available outside of the UK & Ireland.

Application

Penicillin amidase was used to study its effect in release of fatty acid and HSL (homoserine lactone) from AHLs (N -acylhomoserine lactones) in degradation of antibiotics. It was used as positive control for assaying penicillin G acylase activity in the study of functional analysis of bile salt hydrolase and penicillin acylase family members in Lactobacillus sp. Penicillin amidase may be used for synthesis of 6-aminopenicillanic acid from penicillin-G and for the industrial production of β-lactam antibiotics.

Biochem/physiol Actions

The biosynthesis of Penicillin amidase in E. coli by hydrophobic protein chromatography is an inducible reaction which is regulated by metabolized carbon source (e.g. polyols, carboxylic acid etc.). It is also influenced by catabolite repression. It catalyzes the formation of amide bonds through an acyl-enzyme intermediate.

General description

Penicillin amidase is a periplasmic 80K heterodimer with A and B chains (209 and 566 amino acids, respectively). It is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. Among all the sources, the enzyme produced by E. coli is most well-characterized and common for industrial application.

Other Notes

Characterization; In enantioselective resolution; Synthesis of ampicillin and benzylpenicillin

Unit Definition

1 U corresponds to the amount of enzyme which hydrolyzes 1 µmol benzylpenicillin per minute at pH 7.6 and 37°C