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. 1972 Jun;110(3):1073–1081. doi: 10.1128/jb.110.3.1073-1081.1972

Regulation of Valine Catabolism in Pseudomonas putida

Vincent dePaul Marshall 1, John R Sokatch 1
PMCID: PMC247530  PMID: 5030618

Abstract

The activities of six enzymes which take part in the oxidation of valine by Pseudomonas putida were measured under various conditions of growth. The formation of four of the six enzymes was induced by growth on d- or l-valine: d-amino acid dehydrogenase, branched-chain keto acid dehydrogenase, 3-hydroxyisobutyrate dehydrogenase, and methylmalonate semialdehyde dehydrogenase. Branched-chain amino acid transaminase and isobutyryl-CoA dehydrogenase were synthesized constitutively. d-Amino acid dehydrogenase and branched-chain keto acid dehydrogenase were induced during growth on valine, leucine, and isoleucine, and these enzymes were assumed to be common to the metabolism of all three branched-chain amino acids. The segment of the pathway required for oxidation of isobutyrate was induced by growth on isobutyrate or 3-hydroxyisobutyrate without formation of the preceding enzymes. d-Amino acid dehydrogenase was induced by growth on l-alanine without formation of other enzymes required for the catabolism of valine. d-Valine was a more effective inducer of d-amino acid dehydrogenase than was l-valine. Therefore, the valine catabolic pathway was induced in three separate segments: (i) d-amino acid dehydrogenase, (ii) branched-chain keto acid dehydrogenase, and (iii) 3-hydroxyisobutyrate dehydrogenase plus methylmalonate semialdehyde dehydrogenase. In a study of the kinetics of formation of the inducible enzymes, it was found that 3-hydroxyisobutyrate and methylmalonate semialdehyde dehydrogenases were coordinately induced. Induction of enzymes of the valine catabolic pathway was studied in a mutant that had lost the ability to grow on all three branched-chain amino acids. Strain PpM2106 had lowered levels of branched-chain amino acid transaminase and completely lacked branched-chain keto acid dehydrogenase when grown in medium which contained valine. Addition of 2-ketoisovalerate, 2-ketoisocaproate, or 2-keto-3-methylvalerate to the growth medium of strain PpM2106 resulted in induction of normal levels of branched-chain keto acid dehydrogenase; therefore, the branched-chain keto acids were the actual inducers of branched-chain keto acid dehydrogenase.

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Selected References

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

  1. BACHHAWAT B. K., COON M. J., KUPIECKI F. P., NAGLE R., ROBINSON W. G. Coenzyme A thiol esters of isobutyric, methacrylic, and beta-hydroxyisobutyric acids as intermediates in the enzymatic degradation of valine. J Biol Chem. 1957 Jan;224(1):1–11. [PubMed] [Google Scholar]
  2. Bannerjee D., Sanders L. E., Sokatch J. R. Properties of purified methylmalonate semialdehyde dehydrogenase of Pseudomonas aeruginosa. J Biol Chem. 1970 Apr 10;245(7):1828–1835. [PubMed] [Google Scholar]
  3. Brill W. J., Magasanik B. Genetic and metabolic control of histidase and urocanase in Salmonella typhimurium, strain 15-59. J Biol Chem. 1969 Oct 10;244(19):5392–5402. [PubMed] [Google Scholar]
  4. Chasin L. A., Magasanik B. Induction and repression of the histidine-degrading enzymes of Bacillus subtilis. J Biol Chem. 1968 Oct 10;243(19):5165–5178. [PubMed] [Google Scholar]
  5. Dendinger S., Brill W. J. Regulation of proline degradation in Salmonella typhimurium. J Bacteriol. 1970 Jul;103(1):144–152. doi: 10.1128/jb.103.1.144-152.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kemp M. B., Hegeman G. D. Genetic control of the beta-ketoadipate pathway in Pseudomonas aeruginosa. J Bacteriol. 1968 Nov;96(5):1488–1499. doi: 10.1128/jb.96.5.1488-1499.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Marshall V. P., Sokatch J. R. Oxidation of D-amino acids by a particulate enzyme from Pseudomonas aeruginosa. J Bacteriol. 1968 Apr;95(4):1419–1424. doi: 10.1128/jb.95.4.1419-1424.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. NORTON J. E., BULMER G. S., SOKATCH J. R. THE OXIDATION OF D-ALANINE BY CELL MEMBRANES OF PSEUDOMONAS AERUGINOSA. Biochim Biophys Acta. 1963 Oct 8;78:136–147. doi: 10.1016/0006-3002(63)91619-6. [DOI] [PubMed] [Google Scholar]
  9. Newell C. P., Lessie T. G. Induction of histidine-degrading enzymes in Pseudomonas aeruginosa. J Bacteriol. 1970 Oct;104(1):596–598. doi: 10.1128/jb.104.1.596-598.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Norton J. E., Sokatch J. R. Purification and partial characterization of the branched chain amino acid transaminase of Pseudomonas aeruginosa. Biochim Biophys Acta. 1970 May 13;206(2):261–269. doi: 10.1016/0005-2744(70)90109-9. [DOI] [PubMed] [Google Scholar]
  11. Norton J. E., Sokath J. R. Oxidation of D- and L-valine by enzymes of Pseudomonas aeruginosa. J Bacteriol. 1966 Jul;92(1):116–120. doi: 10.1128/jb.92.1.116-120.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  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. PALLERONI N. J., STANIER R. Y. REGULATORY MECHANISMS GOVERNING SYNTHESIS OF THE ENZYMES FOR TRYPTOPHAN OXIDATION BY PSEUDOMONAS FLUORESCENS. J Gen Microbiol. 1964 May;35:319–334. doi: 10.1099/00221287-35-2-319. [DOI] [PubMed] [Google Scholar]
  15. ROBINSON W. G., COON M. J. The purification and properties of beta-hydroxyisobutyric dehydrogenase. J Biol Chem. 1957 Mar;225(1):511–521. [PubMed] [Google Scholar]
  16. Schlesinger S., Scotto P., Magasanik B. Exogenous and endogenous induction of the histidine-degrading enzymes in Aerobacter aerogenes. J Biol Chem. 1965 Nov;240(11):4331–4337. [PubMed] [Google Scholar]
  17. Sokatch J. R., Sanders L. E., Marshall V. P. Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine. J Biol Chem. 1968 May 25;243(10):2500–2506. [PubMed] [Google Scholar]
  18. Taylor R. T., Jenkins W. T. Leucine aminotransferase. I. Colorimetric assays. J Biol Chem. 1966 Oct 10;241(19):4391–4395. [PubMed] [Google Scholar]
  19. YAMADA E. W., JAKOBY W. B. Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A. J Biol Chem. 1960 Mar;235:589–594. [PubMed] [Google Scholar]

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