Titel
Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism
Autor*in
Erika Zangelmi
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma
Francesca Ruffolo
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma
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Abstract
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 N-methyl AEP (M1AEP). Here, we describe a heterogeneous group of FAD-dependent oxidoreductases that efficiently oxidize M1AEP to directly generate PAA, thus expanding the versatility and usefulness of the hydrolytic AEP degradation pathways. Furthermore, some of these enzymes can also efficiently oxidize plain AEP. By doing so, they surrogate the role of PhnW in organisms that do not possess the transaminase and create novel versions of the AEP degradation pathways in which PAA is generated solely by oxidative deamination.
Stichwort
EnzymologyBacteriologyMicrobial metabolism
Objekt-Typ
Sprache
Englisch [eng]
Persistent identifier
Erschienen in
Titel
iScience
Band
26
Ausgabe
11
ISSN
2589-0042
Erscheinungsdatum
2023
Publication
Elsevier BV
Projekt
Kod / Identifikator
P27987-N28
Erscheinungsdatum
2023
Zugänglichkeit
Rechte
Rechteangabe
© 2023 The Author(s)
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