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The crystal structure of isopenicillin N synthase with δ-((L)-α-aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination to iron.

Abstract:

Isopenicillin N synthase (IPNS) catalyses cyclization of δ-(l-α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) to isopenicillin N (IPN), the central step in penicillin biosynthesis. Previous studies have shown that IPNS turns over a wide range of substrate analogues in which the valine residue of its natural substrate is replaced with other amino acids. IPNS accepts and oxidizes numerous substrates that bear hydrocarbon sidechains in this position, however the enzyme is less tolerant of analogues p...

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Publication status:
Published

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Publisher copy:
10.1016/j.abb.2011.09.014

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
Journal:
Archives of biochemistry and biophysics
Volume:
516
Issue:
2
Pages:
103-107
Publication date:
2011-12-05
DOI:
EISSN:
1096-0384
ISSN:
0003-9861
URN:
uuid:2633c46b-9a4b-4541-b067-058aee29b118
Source identifiers:
193277
Local pid:
pubs:193277

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