Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1.
The route of toluene degradation by Pseudomonas mendocina KR1 was studied by separating or purifying from toluene-grown cells the catabolic enzymes responsible for oxidation of p-cresol through the ring cleavage step. Enzymatic transformations corresponding to each of the metabolic steps in the proposed degradative pathway were conducted with cell-free preparations. p-Cresol was metabolized by the enzyme p-cresol methylhydroxylase to p-hydroxybenzaldehyde. p-Hydroxybenzaldehyde was further oxidized by partially purified enzyme preparations to p-hydroxybenzoate and subsequently hydroxylated to form protocatechuate. Protocatechuate was then oxidized by ortho ring cleavage.
Whited
G M
GM
Center for Applied Microbiology, University of Texas, Austin 78712.
Gibson
D T
DT
D000429:Alcohol Oxidoreductases / Q000032:analysis / Q000302:isolation & purification; D000445:Aldehyde Oxidoreductases / Q000032:analysis; D003408:Cresols / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006899:Mixed Function Oxygenases / Q000032:analysis / Q000302:isolation & purification; D011549:Pseudomonas / Q000201:enzymology*; D013057:Spectrum Analysis; D014050:Toluene / Q000378:metabolism*
D003408:Cresols; C032538:4-cresol; D014050:Toluene; D006899:Mixed Function Oxygenases; D000429:Alcohol Oxidoreductases; C021387:3-hydroxybenzyl-alcohol dehydrogenase; C049502:4-cresol dehydrogenase (hydroxylating); D000445:Aldehyde Oxidoreductases; C068611:4-hydroxybenzaldehyde dehydrogenase