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 Hoch, S. O. Articles by Crawford, I. P. Search for Related Content PubMed PubMed Citation Articles by Hoch, S. O. Articles by Crawford, I. P.

 Previous Article  |  Next Article 

J Bacteriol. 1973 November; 116(2): 685-693
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Enzymes of the Tryptophan Pathway in Three Bacillus Species

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

ABSTRACT

The tryptophan synthetic pathway was characterized in three species of Bacillus, B. subtilis, B. pumilus, and B. alvei. They share the common features of a pathway which is subject to tryptophan repression, contains no unexpected complexes among the five enzymes, exhibits dissociable anthranilate synthase enzymes which do not require phosphoribosyl transferase for amidetransfer activity, contains separate indoleglycerol phosphate synthase and phosphoribosylanthranilate isomerase enzymes, and contains similar tryptophan synthetase multimers. In looking at these characteristics in detail however, differences among the three species became apparent, as, for example, in the complementation observed between the and ß₂ components of tryptophan synthetase, and the dissociation patterns of the large and small components of anthranilate synthase. The results demonstrate some pitfalls in attempting to compare multimeric enzymes in crude extracts from different organisms.