The beta-ketoadipate pathway is a chromosomally encoded convergent pat
hway for aromatic compound degradation that is widely distributed in s
oil bacteria and fungi. One branch converts protocatechuate, derived f
rom phenolic compounds including p-cresol, 4-hydroxybenzoate and numer
ous lignin monomers, to beta-ketoadipate. The other branch converts ca
techol, generated from various aromatic hydrocarbons, amino aromatics,
and lignin monomers, also to beta-ketoadipate. Two additional steps a
ccomplish the conversion of beta-ketoadipate to tricarboxylic acid cyc
le intermediates. Enzyme studies and amino acid sequence data indicate
that the pathway is highly conserved in diverse bacteria, including P
seudomonas putida, Acinetobacter calcoaceticus, Agrobacterium tumefaci
ens, Rhodococcus erythropolis, and many others. The catechol branch of
the beta-ketoadipate pathway appears to be the evolutionary precursor
for portions of the plasmid-borne ortho-pathways for chlorocatechol d
egradation. However, accumulating evidence points to an independent an
d convergent evolutionary origin for the eukaryotic beta-ketoadipate p
athway. In the face of enzyme conservation, the beta-ketoadipate pathw
ay exhibits many permutations in different bacterial groups with respe
ct to enzyme distribution (isozymes, points of branch convergence), re
gulation (inducing metabolites, regulatory proteins), and gene organiz
ation. Diversity is also evident in the behavioral responses of differ
ent bacteria to beta-ketoadipate pathway-associated aromatic compounds
. The presence and versatility of transport systems encoded by beta-ke
toadipate pathway regulons is just beginning to be explored in various
microbial groups. It appears that in the course of evolution, natural
selection has caused the beta-ketoadipate pathway to assume a charact
eristic set of features or identity in different bacteria. Presumably
such identities have been shaped to optimally serve the diverse lifest
yles of bacteria.