Abstract
Hydrolysis of p-nitrophenylacetate to p-nitrophenol and acetate and the reversible hydration of CO2 by the zinc metalloenzyme carbonic anhydrase appear to involve similar catalytic mechanisms (Pocker and Sarkanen, 1978). The essential Zn2+ ion at the active site can be replaced by several divalent cations, but only the Zn2+, Co2+, Mn2+, and Cd2+ enzymes retain catalytic activity. The activity of Zn2+ and Co2+ substituted enzmyes is comparable, while that of the Mn2+ and Cd2+ forms is ~ 10% and ~ 30% that of the native enzyme, respectively (Pocker and Sarkanen, 1978).
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Pesando, J.M., Gupta, R.K. (1980). NMR Studies of Carbonic Anhydrase. In: Bauer, C., Gros, G., Bartels, H. (eds) Biophysics and Physiology of Carbon Dioxide. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-67572-0_28
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DOI: https://doi.org/10.1007/978-3-642-67572-0_28
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