PURIFICATION AND CHARACTERIZATION OF CLONED ISOPENICILLIN N SYNTHETASE

JACK E. BALDWIN; STEPHEN J. KILLIN; ANDREW J. PRATT; JOHN D. SUTHERLAND; NICHOLAS J. TURNER; M. JAMES C. CRABBE; EDWARD P. ABRAHAM; ANTHONY C. WILLIS

doi:10.7164/antibiotics.40.652

JACK E. BALDWIN, STEPHEN J. KILLIN, ANDREW J. PRATT, JOHN D. SUTHERLAND, NICHOLAS J. TURNER, M. JAMES C. CRABBE, EDWARD P. ABRAHAM, ANTHONY C. WILLIS

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JOURNAL FREE ACCESS

1987 Volume 40 Issue 5 Pages 652-659

DOI https://doi.org/10.7164/antibiotics.40.652

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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 β-lactam antibiotics in exactly the same way as the fungal protein.

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