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Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a depsipeptide substrate analogue: implications for oxygen binding and a link to nitrile hydratase?

Abstract:

Isopenicillin N synthase (IPNS) is a nonheme iron oxidase that catalyzes the central step in the biosynthesis of beta-lactam antibiotics: oxidative cyclization of the linear tripeptide delta-L-alpha-aminoadipoyl-L-cysteinyl-D-valine (ACV) to isopenicillin N (IPN). The ACV analogue delta-L-alpha-aminoadipoyl-L-cysteine (1-(S)-carboxy-2-thiomethyl)ethyl ester (ACOmC) has been synthesized as a mechanistic probe of IPNS catalysis and crystallized with the enzyme. The crystal structure of the anae...

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Publication status:
Published

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Publisher copy:
10.1021/ja8005397

Authors


Clifton, IJ More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Baldwin, JE More by this author
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Journal:
Journal of the American Chemical Society
Volume:
130
Issue:
31
Pages:
10096-10102
Publication date:
2008-08-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:ffbeaec3-e68d-4c38-b24e-dcb7b119fd0e
Source identifiers:
34308
Local pid:
pubs:34308

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