Journal ArticleOpen Access
DOPA DECARBOXYLASE INHIBITION THROUGH THE INTERACTION OF COENZYME AND SUBSTRATE
Authors
Author Affiliations
University of California, Los Angeles, United States Department of Veterans Affairs, Directorate General of Health Services
Published InJournal of Biological Chemistry
Year1952
Citations151
Abstract
The method of &hales and Schales (1) for obtaining a stable preparation of 3,4-dihydroxyphenyl-n-alanine (L-dopa) decarboxylase has simplified the problem of studying the kinetics of this enzyme system. These authors studied the effect of pH and enzyme concentration on the rate as well as the variation of rate with time. They also showed that pyridoxal-5-phosphate (codecarboxylase) could increase the rate and prolong the reaction. Since their studies were carried out at constant substrate concentration, it seemed desirable to investigate the effect of varying this factor. Preliminary experiments showed, however, that such studies were complicated by a marked substrate inhibition, apparently as a result of interaction of the substrate with the coenzyme. The present paper is a study of the effect…
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