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- W2106788995 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 β 2 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." @default.
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- W2106788995 date "1973-11-01" @default.
- W2106788995 modified "2023-10-14" @default.
- W2106788995 title "Enzymes of the Tryptophan Pathway in Three <i>Bacillus</i> Species" @default.
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- W2106788995 doi "https://doi.org/10.1128/jb.116.2.685-693.1973" @default.
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