Add time:08/13/2019         Source:sciencedirect.com

Crystals of human carbonic anhydrase C were reacted with [14C] bromoacetazolamide and an alkylation was found to occur at the 3′-nitrogen of histidine-64, which is known to be located in the active site region. This reaction requires that the bromomethyl group of the reagent move from its initial binding position, phenylalanine-129, within bonding distance of histidine-64 without significantly disturbing the interaction of the sulfonamide moiety with the active site zinc ion. Since the same histidine has been found previously to react with bromoacetazolamide when the enzyme was in solution, it can be concluded that the conformation of the active site histidine is the same in the two states.

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