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On the structure of histidine and its role in enzyme active sites

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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 ofα-chymotrypsin. It is suggested that the shape of histidine is as important as its pK a for its function at the active sites of enzymes.

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References

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  1. Department of Chemistry, University of Pittsburgh, 15260, Pittsburgh, Pennsylvania, USA

    Julius Rebek Jr.

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  1. Julius Rebek Jr.
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Rebek, J. On the structure of histidine and its role in enzyme active sites. Struct Chem 1, 129–131 (1990). https://doi.org/10.1007/BF00675792

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  • DOI: https://doi.org/10.1007/BF00675792

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