AN INTERPRETATION OF THE KINETIC BEHAVIOR OF MODEL SUBSTRATES OF α-CHYMOTRYPSIN
- 1 September 1961
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 47 (9) , 1341-1355
- https://doi.org/10.1073/pnas.47.9.1341
Abstract
The argument developed in this com-munication has as its goat first, the establishment of generalizations to be used for the interpretation of the kinetic behavior of relatively low molecular weight substrates of alpha-chymotrypsin, and secondly, elaboration of limit cases for a more detailed description of the geometrical disposition and molecular nature of the orienting and binding loci at the active site of the enzyme. The author is of the opinion that the first objective has been achieved for trifunctional substrates R1[image] CONHCHR2COR3, where R2 is not equal to H and the same principles can be applied for substrates for other types and for competitive inhibitors. As for the second objective, it is now possible to suggest a probable conformation for a representative trifunctional substrate at the active site, which in turn provides a partial description of the site itself.Keywords
This publication has 4 references indexed in Scilit:
- The interaction of α-chymotrypsin with α-N-acetyl-l-phenylalaninamidoximeBiochimica et Biophysica Acta, 1961
- The active site of esterasesJournal of Cellular and Comparative Physiology, 1959
- The hydrolysis of peptide and ester bonds by proteolytic enzymesJournal of Cellular and Comparative Physiology, 1959
- Two steps in the reaction of chymotrypsin with acetyl-l-phenylalanine ethyl esterBiochemical Journal, 1955