Enzyme Inhibition in Open Systems: SUPERIORITY OF UNCOMPETITIVE AGENTS
Open Access
- 8 March 1996
- journal article
- research article
- Published by Elsevier BV
- Vol. 271 (10), 5347-5352
- https://doi.org/10.1074/jbc.271.10.5347
Abstract
Investigations of the open system behavior of reversible dead-end inhibitors were carried out by means of computer simulations and experimental studies. The results from both approaches indicate that substrate-competitive inhibition may often be an inappropriate basis for design of potential therapeutic agents. The use of uncompetitive (also called anticompetitive) inhibitors in this role is likely to be far more effective. Chemical analogs of pathogen-specific enzymic reaction products rather than analogs of substrates provide a promising basis for the systematic design of such uncompetitive inhibitors.Keywords
This publication has 16 references indexed in Scilit:
- Thiocyanate and thiosulfateMethods in enzymology, 1987
- Why is uncompetitive inhibition so rare?FEBS Letters, 1986
- A program for the numerical integration of enzyme kinetic equations using small computersInternational Journal of Bio-Medical Computing, 1984
- Thin-layer chromatography of thiosulfonate anionsAnalytical Biochemistry, 1984
- [37] Thiosulfate: Cyanide sulfurtransferase (Rhodanese)Methods in enzymology, 1981
- Purification of thiosulfate sulfurtransferase by selective immobilization on blue agaroseAnalytical Biochemistry, 1978
- Binding Energy, Specificity, and Enzymic Catalysis: The Circe EffectPublished by Wiley ,1975
- The Catalytic and Regulatory Properties of EnzymesAnnual Review of Biochemistry, 1968
- The kinetics of enzyme-catalyzed reactions with two or more substrates or productsBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- KINETIC FORMULATIONS FOR ENZYMIC REACTIONS INVOLVING TWO SUBSTRATESCanadian Journal of Biochemistry and Physiology, 1962