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Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism

Authors :
Erika Zangelmi
Francesca Ruffolo
Tamara Dinhof
Marco Gerdol
Marco Malatesta
Jason P. Chin
Claudio Rivetti
Andrea Secchi
Katharina Pallitsch
Alessio Peracchi
Source :
iScience, Vol 26, Iss 11, Pp 108108- (2023)
Publication Year :
2023
Publisher :
Elsevier, 2023.

Abstract

Summary: 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.

Details

Language :
English
ISSN :
25890042
Volume :
26
Issue :
11
Database :
Directory of Open Access Journals
Journal :
iScience
Publication Type :
Academic Journal
Accession number :
edsdoj.b026c35632e43a0ad50589384f402e1
Document Type :
article
Full Text :
https://doi.org/10.1016/j.isci.2023.108108