- 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...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
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(pdf, 1.2MB)
-
- Publisher copy:
- 10.1002/chem.201701592
-
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- Grant:
- *Grant Number Example*
- Grant:
- *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
- Copyright holder:
- © 2017 McNeill, et al
- Copyright date:
- 2017
- Notes:
- This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Journal article
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
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