Isolation and characterization of catechol 1,2-dioxygenases from Rhodococcus rhodnii strain 135 and Rhodococcus rhodochrous strain 89: comparison with analogous enzymes of the ordinary and modified ortho-cleavage pathways.
Catechol 1,2-dioxygenases of the ordinary ortho-cleavage pathway have been isolated from strains Rhodococcus rhodnii 135 and Rhodococcus rhodochrous 89 grown on phenol as the sole source of carbon and energy. The activities of the catechol 1,2-dioxygenases with 3- and 4-methylpyrocatechols were 1.3-1.5 times higher than those with pyrocatechol. The rate of oxidation of 3-chloropyrocatechol catalyzed by both enzymes was 20% of the rate of oxidation of unsubstituted pyrocatechol. The enzymes are homodimers composed of 37-kD subunits.
Solyanikova
I P
IP
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia.
Golovlev
E L
EL
Lisnyak
O V
OV
Golovleva
L A
LA
D050548:Catechol 1,2-Dioxygenase; D002396:Catechols / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D049308:Dioxygenases; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008970:Molecular Weight; D010105:Oxygenases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012240:Rhodococcus / Q000201:enzymology*; D013045:Species Specificity
D002396:Catechols; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase; C034221:catechol