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. 1987 May;40(5):652-9.
doi: 10.7164/antibiotics.40.652.

Purification and characterization of cloned isopenicillin N synthetase

J E Baldwin, S J Killin, A J Pratt, J D Sutherland, N J Turner, M J Crabbe, E P Abraham, A C Willis
Free article

Purification and characterization of cloned isopenicillin N synthetase

J E Baldwin et al. 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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