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. 1976 Mar;125(3):985–998. doi: 10.1128/jb.125.3.985-998.1976

Metabolism of resorcinylic compounds by bacteria: alternative pathways for resorcinol catabolism in Pseudomonas putida.

P J Chapman, D W Ribbons
PMCID: PMC236175  PMID: 942589

Abstract

Two strains of Pseudomonas putida isolated by enrichment cultures with orcinol as the sole source of carbon were both found to grow with resorcinol. Data are presented which show that one strain (ORC) catabolizes resorcinol by a metabolic pathway, genetically and mechanistically distinct from the orcinol pathway, via hydroxyquinol and ortho oxygenative cleavage to give maleylacetate, but that the other strain (O1) yields mutants that utilize resorcinol. One mutant strain, designated O1OC, was shown to be constitutive for the enzymes of the orcinol pathway. After growth of this strain on resorcinol, two enzymes of the resorcinol pathway are also induced, namely hydroxyquinol 1,2-oxygenase and maleylacetate reductase. Thus hydroxyquniol, formed from resorcinol, undergoes both ortho and meta diol cleavage reactions with the subsequent formation of both pyruvate and maleylacetate. Evidence was not obtained for the expression of resorcinol hydroxylase in strain O1OC; the activity of orcinol hydroxylase appears to be recruited for this hydroxylation reaction. P. putida ORC, on the other hand, possesses individual hydroxylases for orcinol and resorcinol, which are specifically induced by growth on their respective substrates. The spectral changes associated with the enzymic and nonenzymic oxidation of hydroxyquinol are described. Maleylacetate was identified as the product of hydroxyquinol oxidation by partially purified extracts obtained from P. putida ORC grown with resorcinol. Its further metabolism was reduced nicotinamide adenine dinucleotide dependent.

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Selected References

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  1. Chapman P. J., Ribbons D. W. Metabolism of resorcinylic compounds by bacteria: orcinol pathway in Pseudomonas putida. J Bacteriol. 1976 Mar;125(3):975–984. doi: 10.1128/jb.125.3.975-984.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DAGLEY S., CHAPMAN P. J., GIBSON D. T., WOOD J. M. DEGRADATION OF THE BENZENE NUCLEUS BY BACTERIA. Nature. 1964 May 23;202:775–778. doi: 10.1038/202775a0. [DOI] [PubMed] [Google Scholar]
  3. Dagley S. Catabolism of aromatic compounds by micro-organisms. Adv Microb Physiol. 1971;6(0):1–46. doi: 10.1016/s0065-2911(08)60066-1. [DOI] [PubMed] [Google Scholar]
  4. Davey J. F., Ribbons D. W. Metabolism of resorcinylic compounds by bacteria. Purification and properties of acetylpyruvate hydrolase from Pseudomonas putida 01. J Biol Chem. 1975 May 25;250(10):3826–3830. [PubMed] [Google Scholar]
  5. Duxbury J. M., Tiedje J. M., Alexander M., Dawson J. E. 2,4-D metabolism: enzymatic conversion of chloromaleylacetic acid to succinic acid. J Agric Food Chem. 1970 Mar-Apr;18(2):199–201. doi: 10.1021/jf60168a029. [DOI] [PubMed] [Google Scholar]
  6. Evans W. C., Smith B. S., Moss P., Fernley H. N. Bacterial metabolism of 4-chlorophenoxyacetate. Biochem J. 1971 May;122(4):509–517. doi: 10.1042/bj1220509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hopper D. J., Chapman P. J., Dagley S. The enzymic degradation of alkyl-substituted gentisates, maleates and malates. Biochem J. 1971 Mar;122(1):29–40. doi: 10.1042/bj1220029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hopper D. J., Chapman P. J. Gentisic acid and its 3- and 4-methyl-substituted homologoues as intermediates in the bacterial degradation of m-cresol, 3,5-xylenol and 2,5-xylenol. Biochem J. 1971 Mar;122(1):19–28. doi: 10.1042/bj1220019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. KNOX W. E., EDWARDS S. W. The properties of maleylacetoacetate, the initial product of homogentisate oxidation in liver. J Biol Chem. 1955 Oct;216(2):489–498. [PubMed] [Google Scholar]
  10. LACK L. The enzymic oxidation of gentisic acid. Biochim Biophys Acta. 1959 Jul;34:117–123. doi: 10.1016/0006-3002(59)90239-2. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. MASON H. S. The chemistry of melanin; mechanism of the oxidation of catechol by tyrosinase. J Biol Chem. 1949 Dec;181(2):803–812. [PubMed] [Google Scholar]
  13. Ohta Y., Higgins I., Ribbons D. W. Metabolism of resorcinylic compounds by bacteria. Purification and properties of orcinol hydroxylase from Pseudomonas putida 01. J Biol Chem. 1975 May 25;250(10):3814–3825. [PubMed] [Google Scholar]
  14. Ornston L. N. Regulation of catabolic pathways in Pseudomonas. Bacteriol Rev. 1971 Jun;35(2):87–116. doi: 10.1128/br.35.2.87-116.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Stanier R. Y., Ornston L. N. The beta-ketoadipate pathway. Adv Microb Physiol. 1973;9(0):89–151. [PubMed] [Google Scholar]
  16. WALKER P. G. A colorimetric method for the estimation of acetoacetate. Biochem J. 1954 Dec;58(4):699–704. doi: 10.1042/bj0580699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. van der HORST C. Occurrence of keto-acids in blood serum and urine of cattle in comparison with man, horse, sheep and dog. Nature. 1960 Jul 9;187:146–147. doi: 10.1038/187146b0. [DOI] [PubMed] [Google Scholar]

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