Accession Number:

ADA273278

Title:

The Synthesis of Artificial Enzymes

Descriptive Note:

Final rept.

Corporate Author:

COLUMBIA UNIV NEW YORK DEPT OF CHEMISTRY

Personal Author(s):

Report Date:

1993-01-01

Pagination or Media Count:

10.0

Abstract:

A previously reported paper with Chung 1 showed that there can be such a thing as too much rigidity in an enzyme model, and that some freedom of movement must be maintained even though in general flexibility is deleterious in catalysis. The point here is that hydrolysis of an ester by an enzyme such as chymotrypsin requires an interesting geometric change the attacking hydroxyl group of the enzyme must approach in one direction, but then there must be a rotation to permit the second step leading to product. In a cyclodextrin enzyme mimic we had very effective imitation of the first step when there was complete rigid geometric control, but then the second step was slowed. When we incorporated one flexible bond to permit the altered geometry the first step slowed a bit but now the entire process was faster. This gives insight into enzymes themselves, and into optimal design for synthetic catalysts as well.

Subject Categories:

  • Biochemistry
  • Organic Chemistry
  • Physical Chemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE