Affiliation:
1. Department of Microbiology, Scripps Clinic and Research Foundation, La Jolla, California 92038
Abstract
The first four enzymatic activities of the tryptophan synthetic pathway in
Pseudomonas putida
were found on separate molecules. Gel filtration and density gradient centrifugation experiments did not disclose any associations or aggregations among them. These findings contrast with the situation found in the enteric bacteria, where the first two activities are found in an aggregate and the third and fourth are catalyzed by a single enzyme. Tryptophan synthetase, the last enzyme of the pathway, consists of two dissociable components. The affinity of these components is less in
P. putida
than is the case in
Escherichia coli
.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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