Physical Sciences and Mathematics Commons^™

Kinetic, Spectroscopic, And X-Ray Crystallographic Characterization Of The Functional E151h Aminopeptidase From Aeromonas Proteolytica, Krzysztof P. Bzymek, Aaron Moulin, Sabina I. Swierczek, Dagmar Ringe, Gregory A. Petsko, Brian Bennett, Richard C. Holz

Physics Faculty Research and Publications

Glutamate151 (E151) has been shown to be catalytically essential for the aminopeptidase from Vibrio proteolyticus (AAP). E151 acts as the general acid/base during the catalytic mechanism of peptide hydrolysis. However, a glutamate residue is not the only residue capable of functioning as a general acid/base during catalysis for dinuclear metallohydrolases. Recent crystallographic characterization of the d-aminopeptidase from Bacillus subtilis (DppA) revealed a histidine residue that resides in an identical position to E151 in AAP. Because the active-site ligands for DppA and AAP are identical, AAP has been used as a model enzyme to understand the mechanistic role of H115 in …