doi: 10.7164/antibiotics.40.652.
Purification and characterization of cloned isopenicillin N synthetase
- PMID: 3301770
- DOI: 10.7164/antibiotics.40.652
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Purification and characterization of cloned isopenicillin N synthetase
J Antibiot (Tokyo).
1987 May.
Free article
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.
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