Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis

Research has been conducted on phosphonoacetaldehyde hydrolase from Bacillus cereus. This hydrolase catalyzes hydrolytic P-C bond phosphonoacetaldehyde cleavage via Schiff base intermediate formed with Lys53 and the results indicate that ligand binding and dissociation occur from the open conformer and catalysis occurs from the closed conformer.