Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1

J Bacteriol. 1991 May;173(9):3017-20. doi: 10.1128/jb.173.9.3017-3020.1991.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alcohol Oxidoreductases / analysis
  • Alcohol Oxidoreductases / isolation & purification
  • Aldehyde Oxidoreductases / analysis
  • Cresols / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Mixed Function Oxygenases / analysis
  • Mixed Function Oxygenases / isolation & purification
  • Pseudomonas / enzymology*
  • Spectrum Analysis
  • Toluene / metabolism*

Substances

  • Cresols
  • 4-cresol
  • Toluene
  • Mixed Function Oxygenases
  • Alcohol Oxidoreductases
  • 3-hydroxybenzyl-alcohol dehydrogenase
  • 4-cresol dehydrogenase (hydroxylating)
  • Aldehyde Oxidoreductases
  • 4-hydroxybenzaldehyde dehydrogenase