Probing the Conformational States of Thimet Oligopeptidase in Solution.
enzyme kinetics
metallopeptidase
non-canonical amino acid
peptidase family M3
zinc-dependent peptidase
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
30 Jun 2022
30 Jun 2022
Historique:
received:
23
05
2022
revised:
23
06
2022
accepted:
27
06
2022
entrez:
9
7
2022
pubmed:
10
7
2022
medline:
14
7
2022
Statut:
epublish
Résumé
Thimet oligopeptidase (TOP) is a metallopeptidase involved in the metabolism of oligopeptides inside and outside cells of various tissues. It has been proposed that substrate or inhibitor binding in the TOP active site induces a large hinge-bending movement leading to a closed structure, in which the bound ligand is enclosed. The main goal of the present work was to study this conformational change, and fluorescence techniques were used. Four active TOP mutants were created, each equipped with a single-Trp residue (fluorescence donor) and a
Identifiants
pubmed: 35806299
pii: ijms23137297
doi: 10.3390/ijms23137297
pmc: PMC9266445
pii:
doi:
Substances chimiques
Ligands
0
Oligopeptides
0
Metalloendopeptidases
EC 3.4.24.-
thimet oligopeptidase
EC 3.4.24.15
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : São Paulo Research Foundation
ID : 2020/09678-3
Organisme : São Paulo Research Foundation
ID : 2018/09158-0
Organisme : São Paulo Research Foundation
ID : 2014/20847-0
Organisme : São Paulo Research Foundation
ID : 2014/00661-0
Organisme : São Paulo Research Foundation
ID : 2011/20941-9
Organisme : São Paulo Research Foundation
ID : 2011/51989-7
Organisme : Coordenação de Aperfeicoamento de Pessoal de Nível Superior
ID : nuffic 011/09
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