Conformational aspects of inhibitor design: enzyme–substrate interactions in the transition state
- 28 May 1999
- journal article
- review article
- Published by Elsevier in Bioorganic & Medicinal Chemistry
- Vol. 7 (5) , 647-652
- https://doi.org/10.1016/s0968-0896(98)00247-8
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Substrate Connectivity Effects in the Transition State for Cytidine DeaminaseBiochemistry, 1998
- Enzyme−Substrate Complexes of Adenosine and Cytidine Deaminases: Absence of Accumulation of Water AdductsBiochemistry, 1996
- A Proficient EnzymeScience, 1995
- Cytidine Deaminase. The 2·3 Å Crystal Structure of an Enzyme: Transition-state Analog ComplexJournal of Molecular Biology, 1994
- A transition state in pieces: major contributions of entropic effects to ligand binding by adenosine deaminaseBiochemistry, 1992
- Contribution of a single hydroxyl group to transition-state discrimination by adenosine deaminase: evidence for an "entropy trap" mechanismBiochemistry, 1989
- The form of 2-phosphoglycollic acid bound by triosephosphate isomeraseBiochemical and Biophysical Research Communications, 1978
- Enzyme catalysis: Conflicting requirements of substrate access and transition state affinityMolecular and Cellular Biochemistry, 1974
- Changes in absorption spectrum and crystal structure of triose phosphate isomerase brought about by 2-phosphoglycollate, a potential transition state analogueJournal of Molecular Biology, 1970
- XLIV.—On the observation of the course of chemical changeJournal of the Chemical Society, 1867