Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis

The genes encoding phosphonatase in 'Bacillus cereus' and 'Salmonella typhimurium' were cloned for high-level expression in Escherichia coli using mutagenesis and sequenced. The kinetic properties and catalytic pathways of the two purified enzymes were compared. Results suggest that the phosphonatase superfamily scaffold is stable both as an independent unit and as a domain within a larger protein structure and that this scaffold has been used in a variety of combinations as a functional and structural module in the evolution of new protein functions.