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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Enzymes of the beta-ketoadipate pathway are inducible in Rhizobium and Agrobacterium spp. and constitutive in Bradyrhizobium spp.

Protocatechuate is a universal growth substrate for members of the family Rhizobiaceae, and these bacteria utilize the aromatic compound via the beta-ketoadipate pathway. This report describes transcriptional controls exercised by different subgroups of the Rhizobiaceae over five enzymes that catalyze consecutive reactions in the pathway: protocatechuate oxygenase (EC, beta-carboxy-cis,cis-muconate lactonizing enzyme (EC, gamma-carboxymuconolactone decarboxylase (EC, beta-ketoadipate enol-lactone hydrolase (EC, and beta-ketoadipate succinyl-coenzyme A transferase (EC All five enzymes were inducible in the fast-growing strains Agrobacterium rhizogenes, Agrobacterium tumefaciens, Rhizobium fredii, Rhizobium meliloti, Rhizobium leguminosarum, and Rhizobium trifolii. Specific activities in induced cells ranged from 5- to 100-fold greater than those found in uninduced cells. In contrast to the fast-growing strains and members of every other microbial taxon examined to date, the slow-growing Bradyrhizobium japonicum and cowpea Bradyrhizobium spp. constitutively expressed four of the five enzymes; protocatechuate oxygenase was the only inducible enzyme in this group. The slow-growing strains included different DNA homology groups, so it appears likely that constitutive expression of the four enzymes is a common trait in the bradyrhizobia. This property points to the importance of aromatic compounds and aromatic catabolites in the nutrition of these organisms.[1]


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