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

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Abstract
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 1.13.11.3), beta-carboxy-cis,cis-muconate lactonizing enzyme (EC 5.5.1.2), gamma-carboxymuconolactone decarboxylase (EC 4.1.1.44), beta-ketoadipate enol-lactone hydrolase (EC 3.1.1.24), and beta-ketoadipate succinyl-coenzyme A transferase (EC 2.8.3.6). 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.