On the structure of histidine and its role in enzyme active sites |
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Authors: | Julius Rebek Jr. |
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Affiliation: | (1) Department of Chemistry, University of Pittsburgh, 15260 Pittsburgh, Pennsylvania, USA |
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Abstract: | A structural refinement is proposed for the mechanistic details of the action of the serine proteases. The proposal involves ring flipping of the imidazole function of the histidine side chain as a vehicle for proton transfer. The geometric feasibility of this motion is established by molecular graphics analysis of the crystal structure of-chymotrypsin. It is suggested that the shape of histidine is as important as its pKa for its function at the active sites of enzymes. |
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