Journal article
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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Authors
Bibliographic Details
- Journal:
- Chembiochem : a European journal of chemical biology
- Volume:
- 10
- Issue:
- 12
- Pages:
- 2025-2031
- Publication date:
- 2009-08-01
- DOI:
- EISSN:
-
1439-7633
- ISSN:
-
1439-4227
- Source identifiers:
-
34792
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:34792
- UUID:
-
uuid:4221334b-02a0-4883-afac-dc57b7d90fe3
- Local pid:
- pubs:34792
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2009
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