acid-phosphatase and beryllium-fluoride

AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Escherichia coli has revealed the quaternary structure of the enzyme together with hints about its catalytic mechanism. The present work reports the crystal structures of AphA from E. coli in complex with substrate, transition-state, and intermediate analogues. The structures provide new insights into the mechanism of the enzyme and allow a revision of some aspects of the previously proposed mechanism that have broader implications for all the phosphatases of the DDDD superfamily.

Topics: Acid Phosphatase; Adenine; Aluminum Compounds; Aniline Compounds; Beryllium; Catalysis; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Fluorides; Hydrogen Bonding; Multigene Family; Organophosphonates; Organophosphorus Compounds; Protein Structure, Secondary; Substrate Specificity