Discovery of a New, Recurrent Enzyme in Bacterial Phosphonate Degradation: (<i>R</i>)-1-Hydroxy-2-aminoethylphosphonate Ammonia-lyase.

ABSTRACT: Phosphonates represent an important source of bioavailable phosphorus in certain environments. Accordingly, many microorganisms (particularly marine bacteria) possess catabolic pathways to degrade these molecules. One example is the widespread hydrolytic route for the breakdown of 2-aminoethylphosphonate (AEP, the most common biogenic phosphonate). In this pathway, the aminotransferase PhnW initially converts AEP into phosphonoacetaldehyde (PAA), which is then cleaved by the hydrolase PhnX to yield acetaldehyde and phosphate. This work focuses on a pyridoxal 5'-phosphate-dependent enzyme that is encoded in >13% of the bacterial gene clusters containing the phnW-phnX combination. This enzyme (which we termed PbfA) is annotated as a transaminase, but there is no obvious need for an ad

SUBMITTER: Zangelmi E 

PROVIDER: S-EPMC8154272 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature