Abstract
Isopenicillin N synthase is a key enzyme in the biosynthesis of penicillin and cephalosporin antibiotics, catalyzing the oxidative ring closure of δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine to form isopenicillin N. Recent advances in our understanding of the unique chemistry of this enzyme have come through the combined application of spectroscopic, molecular genetic and crystallographic approaches and led to important new insights into the structure and function of this enzyme. Here we review new information on the nature of the endogenous ligands that constitute the ferrous iron active site, sequence evidence for a novel structural motif involved in iron binding in this and related non-heme iron dependent dioxygenases, crystal structure studies on the enzyme and its substrate complex and the impact of these and site-directed mutagenesis studies for unraveling the mechanism of the isopenicillin N synthase reaction.
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Kreisberg-Zakarin, R., Borovok, I., Yanko, M. et al. Recent advances in the structure and function of isopenicillin N synthase. Antonie Van Leeuwenhoek 75, 33–39 (1999). https://doi.org/10.1023/A:1001723202234
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DOI: https://doi.org/10.1023/A:1001723202234