Homologous structural genes and similar induction patterns in Azotobacter spp. and Pseudomonas spp.
Intergeneric comparison of the three enzymes that initiate metabolism of protocatechuate in Azotobacter and Pseudomonas species revealed close immunological relatedness of isofunctional proteins. Furthermore, beta-ketoadipate induces all of the enzymes of the protocatechuate pathway (except protocatechuate oxygenase) in Azotobacter and in Pseudomonas species of the "fluorescent" and "cepacia" groups. This regulatory property sets the organisms apart from other bacteria. Protocatechuate oxygenase from Pseudomonas cepacia, like the enzyme from fluorescent Pseudomonas species, cross-reacts strongly with antiserum prepared against protocatechuate oxygenase from Azotobacter vinelandii. Double-diffusion experiments conducted with the antiserum revealed relatedness of Azotobacter spp. Protocatechuate oxygenases in the following order: A. vinelandii = Azotobacter miscellum greater than Azotobacter chroococcum greater than Azotobacter beijerinkii. The antiserum also revealed serological heterogeneity among Pseudomonas spp. protocatechuate oxygenases which were serologically indistinguishable in earlier studies using Pseudomonas aeruginosa protocatechuate oxygenase as reference protein.
D001395:Azotobacter / Q000235:genetics*; D002262:Carboxy-Lyases / Q000235:genetics / Q000276:immunology; D003429:Cross Reactions; D004790:Enzyme Induction; D005796:Genes; D011520:Protocatechuate-3,4-Dioxygenase / Q000235:genetics / Q000276:immunology; D011549:Pseudomonas / Q000235:genetics*; D013045:Species Specificity
D011520:Protocatechuate-3,4-Dioxygenase; D002262:Carboxy-Lyases; C019832:4-carboxymuconolactone decarboxylase