Hydrolysis of Organophosphate Esters: Phosphotriesterase Activity of Metallo‐β‐lactamase and Its Functional Mimics
作者： A. Tamilselvi , Govindasamy Mugesh
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摘要: The phosphotriesterase (PTE) activity of a series binuclear and mononuclear zinc(II) complexes metallo-beta-lactamase (m beta 1) from Bacillus cereus was studied. complex 1, which exhibits good m 1 activity, shows poor PTE activity. In contrast,complex 2, mimic much higher than replacement Cl- ligands by OH- is important for the high 2 because this does not show any catalytic in methanol. natural enzyme B. also found to be an inefficient catalyst hydrolysis phosphotriesters. These observations indicate that binding beta-lactam substrates at center different Furthermore, phosphodiesters, products triesters, significantly inhibit its functional mimics. Although the mononuclear 3 4 exhibited significant these are almost inactive elimination phosphodiesters reaction site complexes.
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