This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Enatsu, T. Articles by Crawford, I. P. Search for Related Content PubMed PubMed Citation Articles by Enatsu, T. Articles by Crawford, I. P.

 Previous Article  |  Next Article 

J Bacteriol. 1971 October; 108(1): 431-438
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Pseudomonas putida Tryptophan Synthetase

^a Department of Microbiology, Scripps Clinic and Research Foundation, La Jolla, California 92037

ABSTRACT

The two protein components of Pseudomonas putida tryptophan synthetase have been purified to homogeneity. Although there is general similarity between the Pseudomonas enzyme and that of the enteric bacteria, many differences were found. Components from Escherichia coli and P. putida do not stimulate each other enzymatically, and the enzymes differ in their response to monovalent cations. Serine deamination occurs best with the intact enzyme of P. putida, not with the ß₂ subunit alone as in E. coli. The amino acid compositions of the subunits differ appreciably. These findings extend earlier studies showing differences between enteric organisms and pseudomonads in the regulation and genetic organization of the enzymes of the tryptophan pathway.

¹ Present address: Department of Fermentation Technology, Osaka University, Yamada-kami, Suita, Osaka, Japan.