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

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 th

SUBMITTER: Zangelmi E 

PROVIDER: S-EPMC10590968 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature