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. 1968 Feb;106(4):879–885. doi: 10.1042/bj1060879

Catechol oxygenase induction in Pseudomonas aeruginosa

D R Farr 1, R B Cain 1
PMCID: PMC1198591  PMID: 4966085

Abstract

1. The transfer from benzenesulphonate to benzoate as a growth substrate for Pseudomonas aeruginosa strain A resulted in a change in the enzymic route by which catechol was degraded; at intermediate stages it was possible to obtain cells containing the enzymes of both the `ortho' and `meta' metabolic pathways. 2. A similar result was effected by the reverse transfer, benzoate to benzenesulphonate. 3. Catechol itself always elicited a catechol 2,3-oxygenase in uninduced cells, but the product of this reaction, 2-hydroxymuconic semialdehyde, and biochemically related compounds such as 4-hydroxy-2-oxovalerate, unexpectedly induced a catechol 1,2-oxygenase. 4. Both types of catechol oxygenase are strongly repressed by the metabolic end products of both the `ortho' and `meta' pathways, but there was no inhibition of enzymic activity by these end products.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bayly R. C., Dagley S., Gibson D. T. The metabolism of cresols by species of Pseudomonas. Biochem J. 1966 Nov;101(2):293–301. doi: 10.1042/bj1010293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CAIN R. B. The metabolism of protocatechuic acid by a vibrio. Biochem J. 1961 May;79:298–312. doi: 10.1042/bj0790298. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cain R. B., Farr D. R. Metabolism of arylsulphonates by micro-organisms. Biochem J. 1968 Feb;106(4):859–877. doi: 10.1042/bj1060859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DAGLEY S., GIBSON D. T. THE BACTERIAL DEGRADATION OF CATECHOL. Biochem J. 1965 May;95:466–474. doi: 10.1042/bj0950466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Evans W. C. Oxidation of phenol and benzoic acid by some soil bacteria. Biochem J. 1947;41(3):373–382. doi: 10.1042/bj0410373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HAYAISHI O., KATAGIRI M., ROTHBERG S. Studies on oxygenases; pyrocatechase. J Biol Chem. 1957 Dec;229(2):905–920. [PubMed] [Google Scholar]
  7. Hegeman G. D. Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type. J Bacteriol. 1966 Mar;91(3):1140–1154. doi: 10.1128/jb.91.3.1140-1154.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. KAGAN A., DAWBER T. R., KANNEL W. B., REVOTSKIE N. The Framingham study: a prospective study of coronary heart disease. Fed Proc. 1962 Jul-Aug;21(4):52–57. [PubMed] [Google Scholar]
  9. MACDONALD D. L., STANIER R. Y., INGRAHAM J. L. The enzymatic formation of beta-carboxymuconic acid. J Biol Chem. 1954 Oct;210(2):809–820. [PubMed] [Google Scholar]
  10. MANDELSTAM J., JACOBY G. A. INDUCTION AND MULTI-SENSITIVE END-PRODUCT REPRESSION IN THE ENZYMIC PATHWAY DEGRADING MANDELATE IN PSEUDOMONAS FLUORESCENS. Biochem J. 1965 Mar;94:569–577. doi: 10.1042/bj0940569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. NOZAKI M., KAGAMIYAMA H., HAYAISHI O. METAPYROCATECHASE. I. PURIFICATION, CRYSTALLIZATION AND SOME PROPERTIES. Biochem Z. 1963;338:582–590. [PubMed] [Google Scholar]
  12. Ornston L. N., Stanier R. Y. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. J Biol Chem. 1966 Aug 25;241(16):3776–3786. [PubMed] [Google Scholar]
  13. Ornston L. N. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. IV. Regulation. J Biol Chem. 1966 Aug 25;241(16):3800–3810. [PubMed] [Google Scholar]
  14. SISTROM W. R., STANIER R. Y. The mechanism of catechol oxidation by Mycobacterium butyricum. J Bacteriol. 1953 Oct;66(4):404–406. doi: 10.1128/jb.66.4.404-406.1953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Stevenson I. L., Mandelstam J. Induction and multi-sensitive end-product repression in two converging pathways degrading aromatic substances in Pseudomonas fluorescens. Biochem J. 1965 Aug;96(2):354–362. doi: 10.1042/bj0960354. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. TANIUCHI H., KOJIMA Y., KANETSUNA F., OCHIAI H., HAYAISHI O. The mechanism of the autoxidation of oxygenases. Biochem Biophys Res Commun. 1962 Jun 19;8:97–103. doi: 10.1016/0006-291x(62)90243-7. [DOI] [PubMed] [Google Scholar]

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