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. 1973 Nov;116(2):685–693. doi: 10.1128/jb.116.2.685-693.1973

Enzymes of the Tryptophan Pathway in Three Bacillus Species

Sallie O'Neil Hoch 1, Irving P Crawford 1
PMCID: PMC285433  PMID: 4200852

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 α and β2 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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