You are not currently logged in.
Access your personal account or get JSTOR access through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Alternative View of Enzyme Reactions
Michael J. S. Dewar and Donn M. Storch
Proceedings of the National Academy of Sciences of the United States of America
Vol. 82, No. 8 (Apr. 15, 1985), pp. 2225-2229
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/25070
Page Count: 5
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Since adsorption of the substrate in the active site of an enzyme can occur only if all solvent is squeezed out from between them, any reaction between them takes place in the absence of any intervening solvent--i.e., as it would in the gas phase. Recent work has shown that ionic reactions in the gas phase often differ greatly from analogous processes in solution. Therefore, current interpretations of enzyme reactions in terms of solution chemistry are misguided. The large rates and specificity of enzyme reactions may be due simply to elimination of the solvent. The cleavage of peptides by chymotrypsin and carboxypeptidase A can be interpreted satisfactorily in this way.
Proceedings of the National Academy of Sciences of the United States of America © 1985 National Academy of Sciences