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Partially purified subunits of anthranilate synthase were prepared from Bacillus subtilis and Pseudomonas aeruginosa. The large component from B. subtilis (I(B)) complements well with the small component from P. aeruginosa (II(P)) to reconstitute a glutamine-reactive anthranilate synthase. This interaction can be demonstrated with crude extracts from a B. subtilis trpX mutant and a P. aeruginosa trpA mutant. Complementation was also observed with the large component from P. aeruginosa (I(P)) and the small subunit from B. subtilis (II(B)). At saturation the heterologous complex I(B)II(P) has 93% of the activity of the homologous complex I(B)II(B), whereas the hybrid I(P)II(B) is only 22% as active as the homologous complex I(P)II(P).
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