کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1365171 | 981554 | 2008 | 5 صفحه PDF | دانلود رایگان |
The esterase, phosphatase, and sulfatase activities of carbonic anhydrase (CA, EC 4.2.1.1) isozymes, CA I, II, and XIII with 4-nitrophenyl esters as substrates was investigated. These enzymes show esterase activity with 4-nitrophenyl acetate as substrate, with second order rate constants in the range of 753–7706 M−1 s−1, being less effective as phosphatases (kcat/KM in the range of 14.89–1374.40 M−1 s−1) and totally ineffective sulfatases. The esterase/phosphatase activities were inhibited by sulfonamide CA inhibitors, proving that the zinc-hydroxide mechanism responsible for the CO2 hydrase activities of CAs is also responsible for their esterase/phosphatase activity. CA XIII was the most effective esterase and phosphatase. CA XIII might catalyze other physiological reactions than CO2 hydration, based on its relevant phosphatase activity.
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Journal: Bioorganic & Medicinal Chemistry Letters - Volume 18, Issue 7, 1 April 2008, Pages 2267–2271