title: Purification and characterization of cloned isopenicillin N synthetase.
abstract: Isopenicillin N synthetase (IPS) cloned from Cephalosporium acremonium has been isolated from transformed Escherichia coli and purified to homogeneity. The resulting, abundant, recombinant protein, whilst undergoing slightly different N-terminal processing to that observed for the fungally-derived protein, has identical kinetics for the conversion of LLD-aminoadipoyl-cysteinyl-valine to isopenicillin N. Recombinant IPS converts analogue substrates into unusual beta-lactam antibiotics in exactly the same way as the fungal protein.
authors.forename: J E
authors.initials: JE
authors.lastname: Baldwin
authors.forename: S J
authors.initials: SJ
authors.lastname: Killin
authors.forename: A J
authors.initials: AJ
authors.lastname: Pratt
authors.forename: J D
authors.initials: JD
authors.lastname: Sutherland
authors.forename: N J
authors.initials: NJ
authors.lastname: Turner
authors.forename: M J
authors.initials: MJ
authors.lastname: Crabbe
authors.forename: E P
authors.initials: EP
authors.lastname: Abraham
authors.forename: A C
authors.initials: AC
authors.lastname: Willis
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004798:Enzymes / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D004926:Escherichia coli; D009682:Magnetic Resonance Spectroscopy; D010088:Oxidoreductases; D011994:Recombinant Proteins; D013379:Substrate Specificity
chemical_list: D004798:Enzymes; D011994:Recombinant Proteins; D010088:Oxidoreductases; C038370:isopenicillin N synthetase