title: Catalytic scaffolds for phosphoryl group transfer.
abstract: A single genome encodes a large number of phosphoryl hydrolases for the purposes of phosphate recycling, primary and secondary metabolism, signal transduction and regulation, and protection from xenobiotics. Phosphate monoester hydrolysis faces a high kinetic barrier, yet there are multiple solutions to the problem both in terms of catalytic mechanisms and three-dimensional structure of the hydrolases. Recent structural and mechanistic findings highlight the trigonal-bipyramidal nature of the transition state for enzyme promoted phosphate monoester hydrolysis and the evolution and role of inserted loops/domains in governing substrate specificity and promiscuity. Important questions remain as to how electrostatics modulate water networks and critical proton-transfer events. How substrate targeting and catalysis is achieved by the independently evolved catalytic platforms is compared and contrasted in this article.
authors.affiliation: Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA 02215-2521, USA. Electronic address: drkallen@bu.edu.
authors.forename: Karen N
authors.initials: KN
authors.lastname: Allen
authors.affiliation: Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, NM 87131, USA. Electronic address: dd39@unm.edu.
authors.forename: Debra
authors.initials: D
authors.lastname: Dunaway-Mariano
mesh_terms: D055162:Biocatalysis; D006801:Humans; D010710:Phosphates / Q000378:metabolism*; D011522:Protons; D013379:Substrate Specificity
chemical_list: D010710:Phosphates; D011522:Protons