Multichannel resonance Raman experiments on carboxypeptidase A catalyzed ester hydrolysis under cryoenzymological conditions
Two principal reaction pathways have been considered in many laboratories for the action of carboxypeptidase A (CPA) on ester or peptide substrates. In one route, residue Glu-270, an essential active site group, acts as a general base catalyst; in the other pathway, Glu-270 acts as a nucleophile for...
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Published in | Journal of the American Chemical Society Vol. 105; no. 23; pp. 6971 - 6973 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
01.11.1983
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Subjects | |
Online Access | Get full text |
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Summary: | Two principal reaction pathways have been considered in many laboratories for the action of carboxypeptidase A (CPA) on ester or peptide substrates. In one route, residue Glu-270, an essential active site group, acts as a general base catalyst; in the other pathway, Glu-270 acts as a nucleophile forming a transient enzyme-bound mixed anhydride intermediate. The present communication contains results the authors have obtained at low temperatures using multichannel resonance Raman (RR) spectroscopy to ascertain the extent to which acyl-enzyme intermediates accumulate in the CPA-catalyzed hydrolysis of ester substrates. |
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Bibliography: | istex:773BDB150D2C329B6565C042606BF14ACB5BC9DD ark:/67375/TPS-N9S3FWNB-L ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0002-7863 1520-5126 |
DOI: | 10.1021/ja00361a044 |