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J Bacteriol. 1968 January; 95(1): 107-112
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Enzymes of the Tryptophan Synthetic Pathway in Pseudomonas putida

^a 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.

¹ Present address: Department of Fermentation Technology, Osaka University, Osaka, Japan.