Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism
Erika Zangelmi,
Francesca Ruffolo,
Tamara Dinhof,
Marco Gerdol,
Marco Malatesta,
Jason P. Chin,
Claudio Rivetti,
Andrea Secchi,
Katharina Pallitsch,
Alessio Peracchi
Affiliations
Erika Zangelmi
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy
Francesca Ruffolo
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy
Tamara Dinhof
Institute of Organic Chemistry, Faculty of Chemistry, University of Vienna, 1090 Vienna, Austria; Vienna Doctoral School in Chemistry (DoSChem), University of Vienna, 1090 Vienna, Austria
Marco Gerdol
Department of Life Sciences, University of Trieste, Via Giorgieri 5, 34127 Trieste, Italy
Marco Malatesta
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy
Jason P. Chin
School of Biological Sciences and Institute for Global Food Security, Queen’s University Belfast, 19 Chlorine Gardens, BT9 5DL Belfast, UK
Claudio Rivetti
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy
Andrea Secchi
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy
Katharina Pallitsch
Institute of Organic Chemistry, Faculty of Chemistry, University of Vienna, 1090 Vienna, Austria
Alessio Peracchi
Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy; Corresponding author
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.
