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Journal article

Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes.

Abstract:

Penicillin antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both the beta-lactam and thiazolidine rings of the nucleus are created, is mediated by isopenicillin N synthase (IPNS), which binds ferrous iron and uses dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical precedent, IPNS catalyses the transfer of four hydrogen atoms from its tripeptide ...

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Publication status:
Published

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Publisher copy:
10.1038/375700a0

Authors


Clifton, IJ More by this author
Fülöp, V More by this author
Barton, GJ More by this author
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Journal:
Nature
Volume:
375
Issue:
6533
Pages:
700-704
Publication date:
1995-06-05
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
URN:
uuid:f55eefb4-89ce-4931-930b-ff9ad433019e
Source identifiers:
35701
Local pid:
pubs:35701

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