title: Phosphotriesterase: an enzyme in search of its natural substrate.
abstract: The bacterial PTE is able to catalyze the hydrolysis of a wide range of organophosphate nerve agents. The active site has been shown to consist of a unique binuclear metal center that has evolved to deliver hydroxide to the site of bond cleavage. The reaction rate for the hydrolysis of activated substrates such as paraoxon is limited by product release or an associated protein conformational change.
authors.affiliation: Department of Chemistry, Texas A&M University, College Station 77843, USA.
authors.forename: F M
authors.initials: FM
authors.lastname: Raushel
authors.forename: H M
authors.initials: HM
authors.lastname: Holden
mesh_terms: D000595:Amino Acid Sequence; D043303:Aryldialkylphosphatase; D002800:Cholinesterase Inhibitors / Q000378:metabolism; D004950:Esterases / Q000737:chemistry / Q000378:metabolism*; D007306:Insecticides / Q000378:metabolism; D008969:Molecular Sequence Data; D009943:Organophosphorus Compounds; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D002800:Cholinesterase Inhibitors; D007306:Insecticides; D009943:Organophosphorus Compounds; D004950:Esterases; D043303:Aryldialkylphosphatase