Molecular and Cellular Biochemistry

, Volume 3, Issue 3, pp 207–211

Enzyme catalysis: Conflicting requirements of substrate access and transition state affinity

  • Richard Wolfenden

DOI: 10.1007/BF01686645

Cite this article as:
Wolfenden, R. Mol Cell Biochem (1974) 3: 207. doi:10.1007/BF01686645


Maximal efficiency of catalysis appears to require that an enzyme and a substrate combine productively in the ground state. Following this initial combination, powerful forces of attraction are believed to develop between the enzyme and activated forms of the substrate. Local conformation changes may assist this process, if the active site of the enzyme is initially open to substrate access, but tends toenclose the altered substrate in the transition state. In many cases, catalytic complexes must be capable of rapid decomposition by two opposite routes which are not related by symmetry. Structural reorganization of the active site may help to satisfy this additional requirement.

Copyright information

© Dr. W. Junk b.v. Publishers 1974

Authors and Affiliations

  • Richard Wolfenden
    • 1
  1. 1.Department of BiochemistryUniversity of North Carolina Chapel HillNorth CarolinaUSA

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