Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates.
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Innocenti A, Scozzafava A, Parkkila S, Puccetti L, De Simone G, Supuran CT
Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates.
Bioorg Med Chem Lett. 2008 Apr 1;18(7):2267-71. doi: 10.1016/j.bmcl.2008.03.012. Epub 2008 Mar 7.
- PubMed ID
- 18353640 [ View in PubMed]
- Abstract
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 753-7706M(-1)s(-1), being less effective as phosphatases (k(cat)/K(M) in the range of 14.89-1374.40M(-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 CO(2) 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 CO(2) hydration, based on its relevant phosphatase activity.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) Acetazolamide Carbonic anhydrase 1 IC 50 (nM) 330 N/A N/A Details Acetazolamide Carbonic anhydrase 1 IC 50 (nM) 1210 N/A N/A Details Acetazolamide Carbonic anhydrase 2 IC 50 (nM) 28 N/A N/A Details Acetazolamide Carbonic anhydrase 2 IC 50 (nM) 63 N/A N/A Details