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Primary Hydrogen Isotope Effects

  • Chapter
Transition States of Biochemical Processes

Abstract

The important relationship between enzyme catalysis and the enhanced affinity of an enzyme for its substrate in the transition state was first noted by Pauling in 1948.(1) In recent years, attention has been focused on the design of stable analogs of transition states of enzyme reactions, since the structure of high-affinity analogs can provide considerable insight into the structure and energy of enzyme transition states. The factors which give rise to enhanced transition-state analog binding can be complex, however, and many of the analogs which have been tested mimic intermediates rather than true transition states along the enzyme reaction path.(2–5)

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  1. The Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania, USA

    Judith P. Klinman

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  1. Department of Chemistry, Louisiana State University, 70803, Baton Rouge, Louisiana, USA

    Richard D. Gandour

  2. Department of Chemistry, University of Kansas, 66045, Lawrence, Kansas, USA

    Richard L. Schowen

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Klinman, J.P. (1978). Primary Hydrogen Isotope Effects. In: Gandour, R.D., Schowen, R.L. (eds) Transition States of Biochemical Processes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9978-0_4

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