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
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 (M 1 AEP). Here, we describe a heterogeneous group of FAD-dependent oxidoreductases that efficiently oxidize M 1 AEP 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.