ISSN:
1573-1111
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The synthesis and characterization of an artificial acyl-enzyme intermediate of chymotrypsin, and an artificial enzyme, chymotrypsin, are described. They both contain the same three catalytic groups, an imidazolyl group, a hydroxyl group, and a carboxylate ion. In the acyl-enzyme, the three groups are attached to a norbornane backbone, but in the artificial enzyme, the three catalytic groups are attached to a cycloamylose as binder. The artificial acyl-enzyme shows a rate of hydrolysis 154, 000 times faster than an ordinary ester and only 18-fold slower than the real acyl-chymotrypsin. The artificial chymotrypsin is over a thousand fold slower than real chymotrypsin, presumably because of impurities in the preparation.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00662210
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