Bacterial attack on phenolic ethers. Purification and characterization of the components of the meta O-dealkylase of Pseudomonas fluorescens Tp.
The meta O-dealkylase of Pseudomonas fluorescens Tp has been resolved into two protein components, neither of which is a cytochrome. The substrate binding terminal oxidase has been purified and shown to be a non-haem iron protein of approximate molecular weight 118,000, consisting of two seemingly identical subunits, each of molecular weight 55,000. Binding of substrate by the terminal oxidase has been established by difference spectroscopy. The amino acid composition of the protein has also been determined. The NADH-dependent reductase of the system has been partly purified and appears to have a molecular weight of 80,000. The similarity between this and other bacterial O-dealkylases is discussed.
D000596:Amino Acids / Q000032:analysis; D002474:Cell-Free System; D003640:Dealkylation; D062385:Hydroxybenzoates / Q000378:metabolism*; D007501:Iron / Q000032:analysis; D007526:Isoelectric Point; D008970:Molecular Weight; D010088:Oxidoreductases / Q000302:isolation & purification*; D010090:Oxidoreductases, O-Demethylating / Q000302:isolation & purification* / Q000378:metabolism; D010101:Oxygen Consumption; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D014641:Vanillic Acid / Q000378:metabolism*
D000596:Amino Acids; D062385:Hydroxybenzoates; D007501:Iron; D010088:Oxidoreductases; D010090:Oxidoreductases, O-Demethylating; D014641:Vanillic Acid