Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism.
Bacteriology
Enzymology
Microbial metabolism
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
17 Nov 2023
17 Nov 2023
Historique:
received:
16
05
2023
revised:
30
08
2023
accepted:
27
09
2023
medline:
25
10
2023
pubmed:
25
10
2023
entrez:
25
10
2023
Statut:
epublish
Résumé
Phosphonates-compounds containing a direct C-P bond-represent an important source of phosphorus in some environments. The most common natural phosphonate is 2-aminoethylphosphonate (AEP). Many bacteria can break AEP down through specialized "hydrolytic" pathways, which start with the conversion of AEP into phosphonoacetaldehyde (PAA), catalyzed by the transaminase PhnW. However, the substrate scope of these pathways is very narrow, as PhnW cannot process other common AEP-related phosphonates, notably
Identifiants
pubmed: 37876809
doi: 10.1016/j.isci.2023.108108
pii: S2589-0042(23)02185-5
pmc: PMC10590968
doi:
Types de publication
Journal Article
Langues
eng
Pagination
108108Informations de copyright
© 2023 The Author(s).
Déclaration de conflit d'intérêts
The authors declare no competing interests with regard to the content of this study.
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