Publication | Closed Access
Phosphate Ester Hydrolysis: Metal Complexes As Purple Acid Phosphatase and Phosphotriesterase Analogues
111
Citations
155
References
2009
Year
EngineeringChemistryChemical BiologyPurple Acid PhosphataseBioorganometallic ChemistryStructure-function Enzyme KineticsBiological Inorganic ChemistryInorganic ChemistryBiochemistryBiocatalysisCatalysisTriesterase EnzymesProtein PhosphorylationBiomolecular EngineeringNatural SciencesEnzyme CatalysisMetalloproteinPhosphate Ester HydrolysisBimetallic ComplexesMetal Complexes
Abstract This microreview describes the structures and properties of a number of bimetallic complexes designed as both structural and functional mimics of the active sites of some specific metallohydrolase enzymes. The metalloenzymes in question include the predominantly monoesterase‐activity‐displaying purple acid phosphatase (PAP) and di‐ and triesterase enzymes, which have significant roles in the bioremedial hydrolysis of organophosphate pesticides and nerve gases. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)
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