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Terminally truncated isopenicillin N synthase generates a dithioester product: evidence for a thioaldehyde intermediate during catalysis and a new mode of reaction for non-heme iron oxidases

Abstract:

Isopenicillin N synthase (IPNS) catalyses the oxidation of a tripeptide, L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine (ACV), to isopenicillin N (IPN), the first-formed β-lactam in penicillin biosynthesis. IPNS catalysis is dependent upon an iron(II) cofactor and oxygen as co-substrate. In the absence of substrate, the carbonyl oxygen of the side-chain amide of the penultimate residue, Gln330, co-ordinates to the active site metal. Substrate binding ablates this interaction, triggering rearrangem...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1002/chem.201701592

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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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*Grant Number Example*
Publisher:
Wiley Publisher's website
Journal:
Chemistry - A European Journal Journal website
Volume:
23
Issue:
52
Pages:
12815–12824
Publication date:
2017-07-12
Acceptance date:
2017-07-12
DOI:
EISSN:
1521-3765
ISSN:
0947-6539
Pubs id:
pubs:708178
URN:
uri:a315639f-c94d-44e6-808c-992fb5960d31
UUID:
uuid:a315639f-c94d-44e6-808c-992fb5960d31
Local pid:
pubs:708178

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