Molecular dynamics simulations and kinetic measurements provide insights into the structural requirements of substrate size-dependent specificity of oligogalacturonide oxidase 1 (OGOX1).
BBE-Like proteins
Enzyme kinetics
Molecular docking
Molecular dynamics simulations
Oligogalacturonide oxidase (OGOX)
Oligogalacturonides
Substrate specificity
Journal
Plant physiology and biochemistry : PPB
ISSN: 1873-2690
Titre abrégé: Plant Physiol Biochem
Pays: France
ID NLM: 9882449
Informations de publication
Date de publication:
Jan 2023
Jan 2023
Historique:
received:
31
08
2022
revised:
28
10
2022
accepted:
15
11
2022
pubmed:
2
12
2022
medline:
17
1
2023
entrez:
1
12
2022
Statut:
ppublish
Résumé
Oligogalacturonides (OGs) are pectin fragments released from the breakdown of the homogalacturonan during pathogenesis that act as Damage-Associated Molecular Patterns. OG-oxidase 1 (OGOX1) is an Arabidopsis berberine bridge enzyme-like (BBE-l) oligosaccharide oxidase that oxidizes OGs, impairing their elicitor activity and concomitantly releasing H
Identifiants
pubmed: 36455304
pii: S0981-9428(22)00522-8
doi: 10.1016/j.plaphy.2022.11.021
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
Hydrogen Peroxide
BBX060AN9V
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
315-325Informations de copyright
Copyright © 2022 Elsevier Masson SAS. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.