Molecular biology of ?-lactam acylases
- 1 March 1994
- journal article
- Published by Springer Nature in World Journal of Microbiology and Biotechnology
- Vol. 10 (2) , 129-138
- https://doi.org/10.1007/bf00360873
Abstract
β-Lactam acylases such as penicillin G acylases, penicillin V acylases and glutaryl 7-aminocephalosporanic acid acylases are used in the manufacture of 6-aminopenicillanic acid, 7-aminodesacetoxycephalosporanic acid and 7-aminocephalosporanic acid (7-ACA). Genetically-engineered strains producing 1050 U/g, 3200 U/g and 7000 to 10,000 U/I of penicillin G acylase, penicillin V acylase and glutaryl-7-ACA acylase, respectively, have been developed. The penicillin G acylase studied to date and the glutaryl-7-ACA acylase from Pseudomonas sp. share some common features: the active enzyme molecules are composed of two dissimilar subunits that are generated from respective precursor polypeptide; the proteolytic processing is a post-translational modification which is regulated by temperature; and the Ser residue at the N-terminus of the β-sub-unit (Ser290; penicillin G acylase numbering) is implicated as the active site residue. Protein engineering, to generate penicillin G acylase molecules and their precursors with altered sequences, and the structure-function correlation of the engineered molecules are discussed.Keywords
This publication has 43 references indexed in Scilit:
- Molecular aspects of penicillin and cephalosporin acylasesProcess Biochemistry, 1992
- Refolding and assembly of penicillin acylase, an enzyme composed of two polypeptide chains that result from proteolytic activationBiochemistry, 1991
- Direct Production of 7-Aminodeacetylcephalosporanic Acid by Acremonium chrysogenum Hum178.Agricultural and Biological Chemistry, 1991
- Evidence for involvement of arginyl residue at the catalytic site of penicillin acylase from EscherichiacoliBiochemical and Biophysical Research Communications, 1990
- Purification and properties of ampicillin acylase from Pseudomonas melanogenumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Construction and hyperproductivity of engineered strain QE79 bearing recombinant plasmid containing penicillin G acylase gene from Escherichia coli strain AS1.76Biotechnology Letters, 1990
- Thermodynamic profiles of penicillin G hydrolysis catalyzed by wild-type and Met→Ala168 mutant penicillin acylases from Kluyvera citrophilaBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- High cell density continuous culture ofEscherichia coli producing penicillin acylaseBiotechnology Letters, 1988
- The influence of 6-aminopenicillanic acid on antibiotic developmentJournal of Antimicrobial Chemotherapy, 1988
- Sequencing and heterologous expression of the gene encoding penicillin V amidase from Bacillus sphaericusGene, 1986