title: Clues from Xanthomonas campestris about the evolution of aromatic biosynthesis and its regulation.
abstract: The recent placement of major Gram-negative prokaryotes (Superfamily B) on a phylogenetic tree (including, e.g., lineages leading to Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter calcoaceticus) has allowed initial insights into the evolution of the biochemical pathway for aromatic amino acid biosynthesis and its regulation to be obtained. Within this prokaryote grouping, Xanthomonas campestris ATCC 12612 (a representative of the Group V pseudomonads) has played a key role in facilitating deductions about the major evolutionary events that shaped the character of aromatic biosynthesis within this grouping. X. campestris is like P. aeruginosa (and unlike E. coli) in its possession of dual flow routes to both L-phenylalanine and L-tyrosine from prephenate. Like all other members of Superfamily B, X. campestris possesses a bifunctional P-protein bearing the activities of both chorismate mutase and prephenate dehydratase. We have found an unregulated arogenate dehydratase similar to that of P. aeruginosa in X. campestris. We separated the two tyrosine-branch dehydrogenase activities (prephenate dehydrogenase and arogenate dehydrogenase); this marks the first time this has been accomplished in an organism in which these two activities coexist. Superfamily B organisms possess 3-deoxy-D-arabino-heptulosonate 7-P (DAHP) synthase as three isozymes (e.g., in E. coli), as two isozymes (e.g., in P. aeruginosa), or as one enzyme (in X. campestris). The two-isozyme system has been deduced to correspond to the ancestral state of Superfamily B. Thus, E. coli has gained an isozyme, whereas X. campestris has lost one. We conclude that the single, chorismate-sensitive DAHP synthase enzyme of X. campestris is evolutionarily related to the tryptophan-sensitive DAHP synthase present throughout the rest of Superfamily B. In X. campestris, arogenate dehydrogenase, prephenate dehydrogenase, the P-protein, chorismate mutase-F, anthranilate synthase, and DAHP synthase are all allosteric proteins; we compared their regulatory properties with those of enzymes of other Superfamily B members with respect to the evolution of regulatory properties. The network of sequentially operating circuits of allosteric control that exists for feedback regulation of overall carbon flow through the aromatic pathway in X. campestris is thus far unique in nature.
mesh_terms: D010723:3-Deoxy-7-Phosphoheptulonate Synthase / Q000378:metabolism; D000494:Allosteric Regulation; D000878:Anthranilate Synthase / Q000378:metabolism; D005075:Biological Evolution; D002826:Chorismate Mutase / Q000378:metabolism; D005246:Feedback; D010088:Oxidoreductases / Q000378:metabolism; D010649:Phenylalanine / Q000096:biosynthesis*; D011303:Prephenate Dehydrogenase / Q000378:metabolism; D014364:Tryptophan / Q000096:biosynthesis*; D014443:Tyrosine / Q000096:biosynthesis*; D014974:Xanthomonas / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*
chemical_list: D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan; D010088:Oxidoreductases; D011303:Prephenate Dehydrogenase; C027017:cyclohexadienyl dehydrogenase; D010723:3-Deoxy-7-Phosphoheptulonate Synthase; D000878:Anthranilate Synthase; D002826:Chorismate Mutase