Characterization of a cytochrome P450 that catalyzes the O-demethylation of lignin-derived benzoates.
O-demethylation
biocatalysis
crystal structure
cytochrome P450
heme enzyme
lignin
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:
20 Sep 2024
20 Sep 2024
Historique:
received:
31
07
2024
revised:
12
09
2024
accepted:
16
09
2024
medline:
23
9
2024
pubmed:
23
9
2024
entrez:
22
9
2024
Statut:
aheadofprint
Résumé
Cytochromes P450 (P450s) are a superfamily of heme-containing enzymes possessing a broad range of monooxygenase activities. One such activity is O-demethylation, an essential and rate-determining step in emerging strategies to valorize lignin that employ carbon-carbon bond cleavage. We recently identified PbdA, a P450 from Rhodococcus jostii RHA1, and PbdB, its cognate reductase, which catalyze the O-demethylation of para-methoxylated benzoates (p-MBAs) to initiate growth of RHA1 on these compounds. PbdA had the highest affinity (K
Identifiants
pubmed: 39307304
pii: S0021-9258(24)02310-X
doi: 10.1016/j.jbc.2024.107809
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
107809Informations de copyright
Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Conflicts of Interest The authors declare that they have no conflicts of interest with the contents of this article.