Spectroscopic studies reveal details of substrate-induced conformational changes distant from the active site in isopenicillin N synthase.
2-oxoglutarate/α-ketoglutarate oxygenases
DEER/EPR
NMR spectroscopy
catalysis
enzyme catalysis
isopenicillin N synthase
structural dynamics
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
09 2022
09 2022
Historique:
received:
23
03
2022
revised:
06
07
2022
accepted:
07
07
2022
pubmed:
15
7
2022
medline:
30
9
2022
entrez:
14
7
2022
Statut:
ppublish
Résumé
Isopenicillin N synthase (IPNS) catalyzes formation of the β-lactam and thiazolidine rings of isopenicillin N from its linear tripeptide l-δ-(α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) substrate in an iron- and dioxygen (O
Identifiants
pubmed: 35835215
pii: S0021-9258(22)00691-3
doi: 10.1016/j.jbc.2022.102249
pmc: PMC9403350
pii:
doi:
Substances chimiques
Ferrous Compounds
0
Penicillins
0
Thiazolidines
0
Nitric Oxide
31C4KY9ESH
Iron
E1UOL152H7
Oxidoreductases
EC 1.-
Oxygenases
EC 1.13.-
isopenicillin N synthetase
EC 1.21.3.1
penicillin N
NOF9U9EYQ4
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102249Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 106244/Z/14/Z
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M011224/1
Pays : United Kingdom
Organisme : Cancer Research UK
Pays : United Kingdom
Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.