Novel exported fusion enzymes with chorismate mutase and cyclohexadienyl dehydratase activity: Shikimate pathway enzymes teamed up in no man's land.
X-ray crystallography
bacterial metabolism
cooperative active site
enzyme kinetics
exported chorismate mutase
fusion protein
multifunctional enzyme
prephenate dehydratase
shikimate pathway
substrate channeling
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:
Oct 2023
Oct 2023
Historique:
received:
12
04
2023
revised:
29
07
2023
accepted:
11
08
2023
pubmed:
17
8
2023
medline:
17
8
2023
entrez:
16
8
2023
Statut:
ppublish
Résumé
Chorismate mutase (CM) and cyclohexadienyl dehydratase (CDT) catalyze two subsequent reactions in the intracellular biosynthesis of l-phenylalanine (Phe). Here, we report the discovery of novel and extremely rare bifunctional fusion enzymes, consisting of fused CM and CDT domains, which are exported from the cytoplasm. Such enzymes were found in only nine bacterial species belonging to non-pathogenic γ- or β-Proteobacteria. In γ-proteobacterial fusion enzymes, the CM domain is N-terminal to the CDT domain, whereas the order is inverted in β-Proteobacteria. The CM domains share 15% to 20% sequence identity with the AroQ
Identifiants
pubmed: 37586588
pii: S0021-9258(23)02189-0
doi: 10.1016/j.jbc.2023.105161
pmc: PMC10520331
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105161Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflict of interest with the contents of this article.