Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Biochemistry (Mosc). 2009 Sep;74(9):994-1001. doi: 10.1134/s0006297909090077.
The strains Rhodococcus sp. 400, R. rhodochrous 172, and R. opacus 6a utilize 4-methylbenzoate as the only carbon and energy source. 4-Methylcatechol is a key intermediate of biodegradation. Its further conversion by all the strains proceeds via ortho-cleavage. The specific activity of catechol 1,2-dioxygenase assayed in crude extracts of Rhodococcus sp. 400 and R. rhodochrous 172 with 3- and 4-methylcatechols does not exceed the enzyme activity assayed with catechol. Two catechol 1,2-dioxygenases have been purified from the biomass of R. opacus strain 6a grown with 4-methylbenzoate. These enzymes differed in molecular mass and physicochemical and catalytic properties. One of these enzymes belongs to the type of enzymes cleaving the catechol ring and known as methylcatechol 1,2-dioxygenases. In bacteria of the Rhodococcus genus, such an enzyme is described here for the first time.
菌株 Rhodococcus sp. 400、R. rhodochrous 172 和 R. opacus 6a 可将 4-甲基苯甲酸用作唯一的碳源和能源。4-甲基儿茶酚是生物降解的关键中间产物。所有这些菌株进一步通过邻位裂解转化它。用 3-和 4-甲基儿茶酚测定 Rhodococcus sp. 400 和 R. rhodochrous 172 的粗提取物中的儿茶酚 1,2-双加氧酶的比活性不超过用儿茶酚测定的酶活性。已经从用 4-甲基苯甲酸培养的 R. opacus 菌株 6a 的生物质中纯化出两种儿茶酚 1,2-双加氧酶。这些酶在分子量以及物理化学和催化特性上有所不同。其中一种酶属于裂解儿茶酚环的酶,称为甲基儿茶酚 1,2-双加氧酶。在 Rhodococcus 属的细菌中,这里首次描述了这种酶。