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Structural studies on the reaction of isopenicillin N synthase with a sterically demanding depsipeptide substrate analogue.

Abstract:

Isopenicillin N synthase (IPNS) is a nonheme iron(II)-dependent oxidase that catalyses the central step in penicillin biosynthesis, conversion of the tripeptide delta-L-alpha-aminoadipoyl-L-cysteinyl-D-valine (ACV) to isopenicillin N (IPN). This report describes mechanistic studies using the analogue delta-(L-alpha-aminoadipoyl)-(3S-methyl)-L-cysteine D-alpha-hydroxyisovaleryl ester (A(S)mCOV), designed to intercept the catalytic cycle at an early stage. A(S)mCOV incorporates two modification...

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Publication status:
Published

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Publisher copy:
10.1002/cbic.200900080

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
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Journal:
Chembiochem : a European journal of chemical biology
Volume:
10
Issue:
12
Pages:
2025-2031
Publication date:
2009-08-05
DOI:
EISSN:
1439-7633
ISSN:
1439-4227
URN:
uuid:4221334b-02a0-4883-afac-dc57b7d90fe3
Source identifiers:
34792
Local pid:
pubs:34792

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