Abstract
A pyrocatechase was isolated from a strain of Brevibacterium fuscum and purified about 40-fold. This enzyme was homogeneous by ultracentrifugation. Its molecular weight was estimated as 78, 000.
Brevibacterium pyrocatechase has unique substrate specificity. Thus it catalyzes the oxidative cleavage of the benzene ring of various catechols including 3- and 4-methyl-catechols and pyrogallol unlike the pyrocate-chases from other bacterial species.
The purified enzyme requires both ferrous ion and a reducing agent for maximal activity.
The reaction products from catechol, 3-and 4-methylcatechols and pyrogallol were identified as cis, cis-muconic acid, α- and β-methylmuconic acids and α-hydroxymuconic acid, respectively.
It was also demonstrated that the substrate specificity of the enzyme obtained from Brevibacterium fuscum was the same on what-ever metabolic precursors of catechol the bacteria were grown.
We are indebted to Dr. S. Senoh for his many stimulating discussions and suggestions during the course of this work.
