Purification and properties of protocatechuate 3,4-dioxygenase from Chaetomium piluliferum induced with p-hydroxybenzoic acid.
1. Protocatechuate 3,4-dioxygenase (protocatechuate : oxygen 3,4-oxidoreductase, EC 1.13.11.3) was isolated from mycelium of Chaetomium piluliferum induced with p-hydroxybenzoic acid. The enzyme was purified about 80-fold by ammonium sulphate fractionation and DEAE-cellulose and Sephadex G-200 chromatography, and was homogeneous on polyacrylamide-gel electrophoresis. 2. The enzyme showed high substrate specificity; its pH optimum was 7.5-8.0, and molecula weight about 76 000 as determined by filtration on Sephadex G-200. The Michaelis constant for protocatechuic acid was 11.1 microM.
D001203:Ascomycota / Q000201:enzymology*; D002597:Chaetomium / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D006863:Hydrogen-Ion Concentration; D062385:Hydroxybenzoates; D008970:Molecular Weight; D010105:Oxygenases / Q000302:isolation & purification*; D010226:Parabens / Q000494:pharmacology; D011520:Protocatechuate-3,4-Dioxygenase / Q000096:biosynthesis / Q000302:isolation & purification*; D013268:Stimulation, Chemical
D062385:Hydroxybenzoates; D010226:Parabens; C009091:protocatechuic acid; D010105:Oxygenases; D011520:Protocatechuate-3,4-Dioxygenase