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The subunits of anthranilate synthase were separated and partially purified by Sephadex G-100 gel filtration from the following six species ofBacillus :Bacillus subtilis, Bacillus licheniformis, Bacillus alvei, Bacillus coagulans, Bacillus pumilus , andBacillus mascerans . Our data suggest that the enzyme fromB. alvei is unique among these species. First, the anthranilate synthase complexes are readily dissociated during gel filtration in the absence of glutamine into a large component (aminotransferase), subunit E, and a small component subunit X (glutamine-binding protein), whereas a higher salt concentration is required to dissociate the complex fromB. alvei . Second, the aminotransferase activity from all six species is stimulated by glycerol and inhibited by tryptophan; however, only the large component fromB. alvei is stimulated by 2-mercaptoethanol. Finally, the large component can be titrated with the small component to yield a complex which can utilize glutamine as a substrate (amidotransferase). The homologous complexes have an amidotransferase to aminotransferase ratio of 1.4 to 2.3, but theB. alvei complex has a ratio of 0.9. Except for complexes that involve the large component fromB. alvei , hybrid complexes can be formed which have ratios as good as the homologous complexes. These data are consistent with the hypothesis thatB. alvei is unique among the bacilli with respect to some enzymes in the aromatic amino acid biosynthetic pathway.

Homologous and Hybrid Complexes of Anthranilate Synthase from Bacillus Species