Recent advances in the structure and function of isopenicillin N synthase

Rachel Kreisberg-Zakarin, Ilya Borovok, Michaela Yanko, Yair Aharonowitz, Gerald Cohen*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

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 isopeniciliin 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.

Original languageEnglish
Pages (from-to)33-39
Number of pages7
JournalAntonie van Leeuwenhoek
Volume75
Issue number1-2
DOIs
StatePublished - 1999

Funding

FundersFunder number
Felix Frolow
IPNS
University of Oregon
Israel Science Foundation488/97
Tel Aviv University

    Keywords

    • Active site
    • Crystal structure
    • Iron binding motif
    • Isopenicillin N synthase
    • Mechanism of action

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