Evolutionary and structural analyses of the NADPH oxidase family in eukaryotes reveal an initial calcium dependency.
Enzyme evolution
NADPH oxidase
NOX
Reactive oxygen species
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
10 2022
10 2022
Historique:
received:
01
07
2022
revised:
04
08
2022
accepted:
08
08
2022
pubmed:
24
8
2022
medline:
28
9
2022
entrez:
23
8
2022
Statut:
ppublish
Résumé
Reactive oxygen species are unstable molecules generated by the partial reduction of dioxygen. NADPH oxidases are a ubiquitous family of enzymes devoted to ROS production. They fuel an array of physiological roles in different species and are chemically demanding enzymes requiring FAD, NADPH and heme prosthetic groups in addition to either calcium or a various number of cytosolic mediators for activity. These activating partners are exclusive components that partition and distinguish the NOX members from one another. To gain insight into the evolution of these activating mechanisms, and in general in their evolutionary history, we conducted an in-depth phylogenetic analysis of the NADPH oxidase family in eukaryotes. We show that all characterized NOXs share a common ancestor, which comprised a fully formed catalytic unit. Regarding the activation mode, we identified calcium-dependency as the earliest form of NOX regulation. The protein-protein mode of regulation would have evolved more recently by gene-duplication with the concomitant loss of the EF-hands motif region. These more recent events generated the diversely activated NOX systems as observed in extant animals and fungi.
Identifiants
pubmed: 35998431
pii: S2213-2317(22)00208-7
doi: 10.1016/j.redox.2022.102436
pmc: PMC9421330
pii:
doi:
Substances chimiques
Reactive Oxygen Species
0
Flavin-Adenine Dinucleotide
146-14-5
Heme
42VZT0U6YR
NADP
53-59-8
NADPH Oxidase 1
EC 1.6.3.-
NADPH Oxidase 4
EC 1.6.3.-
NADPH Oxidases
EC 1.6.3.-
Oxygen
S88TT14065
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102436Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The Authors declare no conflicts of interest.