Structural highlights
Function
PEPQ_ECOLI Splits dipeptides with a prolyl residue in the C-terminal position and a polar or nonpolar amino acid at the N-terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX.[1]
References
- ↑ Park MS, Hill CM, Li Y, Hardy RK, Khanna H, Khang YH, Raushel FM. Catalytic properties of the PepQ prolidase from Escherichia coli. Arch Biochem Biophys. 2004 Sep 15;429(2):224-30. PMID:15313226 doi:http://dx.doi.org/10.1016/j.abb.2004.06.022