Hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle.
作者： C K Tu , H G Thomas , G C Wynns , D N Silverman
DOI: 10.1016/S0021-9258(18)67496-4
关键词:
摘要: We report three experiments which show that the hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle occurs at a site on enzyme different than active for CO2 hydration. This is in contrast with isozymes I and II sites hydration are same. The pH profile kcat/Km was roughly described ionization group pKa 6.5, whereas isozyme independent range 6.0-8.5. apoenzyme III, inactive catalytic CO2, found to be as native III. Concentrations N-3 OCN- sulfonamides methazolamide chlorzolamide inhibited did not affect
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