| Type: | Family | Name: | Phosphonoacetaldehyde hydrolase |
| Description: | Phosphonoacetaldehyde hydrolase or phosphonatase catalyses the cleavage of the carbon-phosphorous bond of a phosphonate.This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases, and contains a modified version of the conserved catalytic motifs of that superfamily []. The first motif is usually DxDx(T/V); here it is DxAxT. In the third motif the normally conserved lysine is instead an arginine. Additionally, the enzyme from Bacillus cereuscontains a unique conserved catalytic lysine which is involved in the binding and activation of the substrate through the formation of a Schiff base [].The substrate of this enzyme is the product of 2-aminoethylphosphonate (AEP) transaminase, phosphonoacetaldehyde. This degradation pathway for AEP may be related to its toxic properties which are utilised by microorganisms as a chemical warfare agent. | Short Name: | Phosphonoacetald_hydro |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Pp3s34_170V3.1.p | PAC:32948266 | Physcomitrium patens |
1778
 |
|
| Pp3s34_610V3.1.p | PAC:32948312 | Physcomitrium patens |
2078
|
