Purification and characterization of cloned isopenicillin N synthetase.
- 31 December 1986
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 40 (5) , 652-659
- https://doi.org/10.7164/antibiotics.40.652
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.This publication has 9 references indexed in Scilit:
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