The enzyme apparatus involved in the catabolism of aromatic compounds in rhodococci is characterized by the presence of pyrocatechase and protocatechoate-3,4-dioxygenase as principal enzymes cleaving the aromatic cycle. Metapyrocatechase was found in about 30% of the rhodococci. All the enzymes are inducible. The inductor of pyrocatechase seems to be cyc-cys-muconate, and that of protocatechase appears to be 3-oxoadipate. The metapyrocatechase of rhodococci, in contrast to that of Pseudomonas, is not induced by benzoate, p-toluylate, p-xylene and phenol. The activity of metapyrocatechase rises 20-50 times comparing to the basal level only in the presence of p-cresol. The enzyme has a relatively low activity in rhodococci (50-200 nmole per 1 min per 1 mg of protein), though a very high affinity for methylcatechols. The activity of metapyrocatechase with methylcatechols is 2-5 times as high as that with catechol as a substrate, whereas the activity of pyrocatechase with methylcatechols is two times as low as that with catechol as a substrate. Such additional substrates as acetate, glycerol or fumarate have no effect on the qualitative composition of the key enzymes involved in the degradation of aromatic compounds in Rhodococcus carollinus 172. Glucose represses the synthesis of enzymes cleaving the aromatic ring by 100%. Fumarate taken in a 5-fold excess inhibits the activity of catechol oxygenases by 40%; if it is taken in a 1000-fold excess, it inhibits the enzyme activity by 100%.