Abstract
Investigation of a mutant strain of Pseudomonas putida NCIB 10015, strain PsU-E1, showed that it had lost the ability to produce catechol 1,2-oxygenase after growth with catechol. Additional mutants of both wild-type and mutant strains PsU-E1 have been isolated that grow on catechol, but not on benzoate, yet still form a catechol 1,2-oxygenase when exposed to benzoate. These findings indicate that either there are separately induced catechol 1,2-oxygenase enzymes, or that there are two separate inducers for the one catechol 1,2-oxygenase enzyme. Comparisons of the physical properties of the catechol 1,2-oxygenases formed in response to the two different inducers show no significant differences, so it is more probable that the two proteins are the product of the same gene. Sufficient enzymes of the ortho-fission pathway are induced in the wild-type strain by the initial substrate benzoate (or an early intermediate) to commit that substrate to metabolism by ortho fission exclusively. A mechanism exists that permits metabolism of catechol by meta fission if the ortho-fission enzymes are unable to prevent its intracellular accumulation.
Full text
PDF









Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bayly R. C., Wigmore G. J. Metabolism of phenol and cresols by mutants of Pseudomonas putida. J Bacteriol. 1973 Mar;113(3):1112–1120. doi: 10.1128/jb.113.3.1112-1120.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Collinsworth W. L., Chapman P. J., Dagley S. Stereospecific enzymes in the degradation of aromatic compounds by pseudomonas putida. J Bacteriol. 1973 Feb;113(2):922–931. doi: 10.1128/jb.113.2.922-931.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Farr D. R., Cain R. B. Catechol oxygenase induction in Pseudomonas aeruginosa. Biochem J. 1968 Feb;106(4):879–885. doi: 10.1042/bj1060879. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Feist C. F., Hegeman G. D. Phenol and benzoate metabolism by Pseudomonas putida: regulation of tangential pathways. J Bacteriol. 1969 Nov;100(2):869–877. doi: 10.1128/jb.100.2.869-877.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Feist C. F., Hegeman G. D. Regulation of the meta cleavage pathway for benzoate oxidation by Pseudomonas putida. J Bacteriol. 1969 Nov;100(2):1121–1123. doi: 10.1128/jb.100.2.1121-1123.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]
- Murray K., Williams P. A. Role of catechol and the methylcatechols as inducers of aromatic metabolism in Pseudomonas putida. J Bacteriol. 1974 Mar;117(3):1153–1157. doi: 10.1128/jb.117.3.1153-1157.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nakazawa T., Yokota T. Benzoate metabolism in Pseudomonas putida(arvilla) mt-2: demonstration of two benzoate pathways. J Bacteriol. 1973 Jul;115(1):262–267. doi: 10.1128/jb.115.1.262-267.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ornston L. N., Ornston M. K., Chou G. Isolation of spontaneous mutant strains of Pseudomonas putida. Biochem Biophys Res Commun. 1969 Jul 7;36(1):179–184. doi: 10.1016/0006-291x(69)90666-4. [DOI] [PubMed] [Google Scholar]
- Ornston L. N. The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway. J Biol Chem. 1966 Aug 25;241(16):3795–3799. [PubMed] [Google Scholar]
- 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]
- Reiner A. M. Metabolism of benzoic acid by bacteria: 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid is an intermediate in the formation of catechol. J Bacteriol. 1971 Oct;108(1):89–94. doi: 10.1128/jb.108.1.89-94.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sala-Trepat J. M., Evans W. C. The meta cleavage of catechol by Azotobacter species. 4-Oxalocrotonate pathway. Eur J Biochem. 1971 Jun 11;20(3):400–413. doi: 10.1111/j.1432-1033.1971.tb01406.x. [DOI] [PubMed] [Google Scholar]
- Stanier R. Y., Ornston L. N. The beta-ketoadipate pathway. Adv Microb Physiol. 1973;9(0):89–151. [PubMed] [Google Scholar]
- Treccani V., Galli E., Catelani D., Sorlini C. Induction of 1,2- and 2,3-diphenol oxygenases in Pseudomonas desmolyticum. Z Allg Mikrobiol. 1968;8(1):65–69. doi: 10.1002/jobm.3630080108. [DOI] [PubMed] [Google Scholar]
- Wigmore G. J., Bayly R. C. A mutant of Pseudomonas putida with altered regulation of the enzymes for degradation of phenol and cresols. Biochem Biophys Res Commun. 1974 Sep 9;60(1):48–55. doi: 10.1016/0006-291x(74)90170-3. [DOI] [PubMed] [Google Scholar]
- Wigmore G. J., Bayly R. C., Di Berardino D. Pseudomonas putida mutants defective in the metabolism of the products of meta fission of catechol and its methyl analogues. J Bacteriol. 1974 Oct;120(1):31–37. doi: 10.1128/jb.120.1.31-37.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Williams P. A., Catterall F. A., Murray K. Metabolism of naphthalene, 2-methylnaphthalene, salicylate, and benzoate by Pseudomonas PG: regulation of tangential pathways. J Bacteriol. 1975 Nov;124(2):679–685. doi: 10.1128/jb.124.2.679-685.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Williams P. A., Murray K. Metabolism of benzoate and the methylbenzoates by Pseudomonas putida (arvilla) mt-2: evidence for the existence of a TOL plasmid. J Bacteriol. 1974 Oct;120(1):416–423. doi: 10.1128/jb.120.1.416-423.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
