Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase.
作者： Sarah D. Aubert , Yingchun Li , Frank M. Raushel
DOI: 10.1021/BI0497805
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摘要: Phosphotriesterase (PTE) from Pseudomonas diminuta is a zinc metalloenzyme that hydrolyzes variety of organophosphorus compounds. The kinetic parameters Zn/Zn PTE, Cd/Cd and mixed-metal Zn/Cd hybrid PTE were obtained with substrates to determine the role each metal ion in binding catalysis. pH-rate profiles for hydrolysis diethyl p-nitrophenyl phosphate (I) p-chlorophenyl (II) demonstrated ionization single group pH range 5−10 was critical substrate turnover. pKa values determined assays dependent on identity occupied α site within binuclear center. These results suggest hydrolytic nucleophile activated as hydroxide via water molecule attached α-metal ion. constants II thiophosphate (IV) substituted forms PTE. kineti...
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