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

  • G M Whited
    Center for Applied Microbiology, University of Texas, Austin 78712.
  • D T Gibson
    Center for Applied Microbiology, University of Texas, Austin 78712.

書誌事項

公開日
1991-05
権利情報
  • https://journals.asm.org/non-commercial-tdm-license
DOI
  • 10.1128/jb.173.9.3017-3020.1991
公開者
American Society for Microbiology

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説明

<jats:p>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.</jats:p>

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