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76427 Sigma-Aldrich

Penicillin Amidase from Escherichia coli

5-10 units/mg protein

Synonym: Penicillin Acylase, Penicillin Amidohydrolase



Related Categories 3.5.x.x Acting on C-N other than peptides, 3.x.x.x Hydrolases, Biochemicals and Reagents, Cell Biology, Enzyme Class Index,
Quality Level   100
form   suspension
specific activity   5-10 units/mg protein
mol wt   Mr ~70000
storage temp.   2-8°C


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.


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.

Unit Definition

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

Other Notes

Characterization; In enantioselective resolution; Synthesis of ampicillin and benzylpenicillin

Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable


Certificate of Analysis (COA)

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Protocols & Articles

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