Phosphonoacetaldehyde hydrolase

Phosphonoacetaldehyde hydrolase is a bacterial enzyme that catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate, breaking a stable carbon-phosphorus (C-P) bond. It plays a key role in the metabolism of organophosphonates, particularly as part of the 2-aminoethylphosphonate degradation pathway in certain microorganisms such as Bacillus cereus. The enzyme acts via a mechanism involving imine (Schiff base) formation with a lysine residue in the active site, labilizing the C-P bond. It requires magnesium as a cofactor and belongs to the haloacid dehalogenase (HAD) superfamily. There are no known drugs targeting this bacterial enzyme, and it is not considered a therapeutic target in humans. Its primary biological relevance is in microbial phosphorus metabolism rather than direct clinical implications.

Other names

phosphonatase2-phosphonoacetylaldehyde phosphonohydrolase2-oxoethylphosphonate phosphonohydrolase