Affiliation:
1. Department of Biochemistry, University of British Columbia, Vancouver 8, B.C., Canada
Abstract
Acetolactate formation in Escherichia coli B results from the activity of a single system, acetohydroxy acid synthetase, which has a pH optimum of 8·0 and is sensitive to end-product inhibition by l-valine. Acetohydroxy acid synthetase was found to be subject to catabolite repression, and the nature and concentration of the carbon source had a greater effect on the formation of the enzyme than had the known end products (valine, isoleucine, leucine and pantothenate) of the biosynthetic pathways of which this enzyme is a member. The results suggest that acetohydroxy acid synthetase may play an amphibolic role in E. coli B.
Cited by
11 articles.
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