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NMR Studies of Carbonic Anhydrase

  • J. M. Pesando
  • R. K. Gupta
Conference paper
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

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).

Keywords

Carbonic Anhydrase Nuclear Magnetic Relaxation Paramagnetic Effect Proton Resonance Frequency Human Carbonic Anhydrase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1980

Authors and Affiliations

  • J. M. Pesando
    • 1
  • R. K. Gupta
    • 2
  1. 1.Sidney Farber Cancer InstituteHarvard Medical SchoolBostonUSA
  2. 2.The Institute for Cancer ResearchThe Fox Chase Cancer CenterPhiladelphiaUSA

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