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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Fisher, J. R. Barber, A. K. |
| Abstract | In an attempt to gain a better understanding of the mechanism of action of carboxypeptidase A (EC 3.4.2.1), many kinetic studies have been undertaken using numerous substrates-both esters and peptides-that have exhibited substrate linearity, inhibition, activation, and sigmoid-shaped rate plots. Numerous interpretations of the kinetic data have been proposed, none of which are fully in accord both with kinetic data and x-ray crystallographic studies. Much of the kinetic data has been interpreted using multisite binding while the x-ray information seems to severely restrict these possibilities. We have examined the feasibility of a simple model with a single active site, without modifier sites, that allows only one substrate molecule to bind the enzyme at a time. A random-pathway model was identified that simultaneously accounts for the nonlinear kinetic data and meets the restrictions imposed by the x-ray crystallographic studies. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 10 |
| Volume Number | 69 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1972-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Carboxypeptidases Binding Sites Chemical Phenomena Chemistry Crystallography Esters Hydrolysis Kinetics Models, Chemical Peptides Protein Binding Protein Conformation Structure-Activity Relationship Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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