Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1
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- G M Whited
- Center for Applied Microbiology, University of Texas, Austin 78712.
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- 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
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- https://journals.asm.org/non-commercial-tdm-license
- DOI
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- 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>
収録刊行物
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- Journal of Bacteriology
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Journal of Bacteriology 173 (9), 3017-3020, 1991-05
American Society for Microbiology