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Volume 23, Issue 2

The Oxidation of Tricarboxylic Acid Cycle Intermediates by a Strain of Free

Abstract

SUMMARY: Washed suspensions of strain 142, grown on a yeast extract medium, were unable to oxidize some members of the tricarboxylic acid cycle immediately unless these compounds had been added to the growth medium. At 25° the organism eventually acquired the ability to oxidize these compounds; with succinate rapid oxidation was not obtained even after 6 hr. Rapid oxidation of succinate did occur when washed suspensions were incubated first with - or -malate. The lag periods were shortened by the addition of ammonium sulphate, but adaptation was prevented by chloramphenicol, 2:4-dinitrophenol, azide or an increase in temperature to 37°. Neither chloramphenicol nor the increase in temperature affected oxidation by adapted organisms; 2:4-dinitrophenol and azide were inhibitory, especially when added with the substrate. Extracts of unadapted organisms oxidized immediately all those compounds which intact organisms did not. Chloramphenicol and the respiratory uncoupling agents did not inhibit oxidations by the cell extracts. Extracts from adapted or unadapted bacteria reacted with succinate, malate and fumarate in the presence of hydroxylamine to form substances which gave coloured compounds with ferric chloride. The compounds with fumarate and malate were not identified. These compounds and succinhydroxa- mate were formed equally well by extracts of organisms grown in the absence or presence of the dicarboxylic acids. There was no evidence that the enzymes responsible for these reactions are directly concerned with the penetration of the acids into .

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© Society for General Microbiology 1960
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1960-10-01
2024-05-03
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References

  1. Barrett J. T., Larsen A. D., Kallio R. E. 1953; The nature of the adaptive lag of Pseudomonas fluorescens toward citrate. J. Bact 65:187
     [Google Scholar]
  2. Berg P. 1956; Acyl adenylates: the interaction of adenosine triphosphate and l- methionine. J. biol. Chem 222:1025
     [Google Scholar]
  3. Clarke P. H., Meadow P. M. 1959; Evidence for the occurrence of permeases for tricarboxylic acid cycle intermediates in Pseudomonas aeruginosa . J. gen. Microbiol 20:144
     [Google Scholar]
  4. Cohn D. V. 1956; The oxidation of malic acid by Micrococcus lysodeikticus. . J. biol. Chem 221:413
     [Google Scholar]
  5. Dagley S., Fewster M. E., Happold F. C. 1952; The bacterial oxidation of phenyl- acetic acid. J. Bact 63:327
     [Google Scholar]
  6. Davis B. D. 1956 In Enzymes: Units of Biological Structure and Function p. 509 Gaebler O. Ed. New York: Academic Press Inc.;
     [Google Scholar]
  7. Elliott W. H. 1956; The enzymic activation of cholic acid by guinea-pig-liver micro-somes. Biochem. J 62:427
     [Google Scholar]
  8. Friedemann T. E., Haugen G. E. 1943; Pyruvic acid. II. The determination of keto acids in blood and urine. J. biol. Chem 147:415
     [Google Scholar]
  9. Goucher C. R., Woodside E. E., Kocholaty W. 1954; The influence of dinitro- phenol on the oxidation of acetate and succinate by Escherichia coli . J. Bact 67:593
     [Google Scholar]
  10. Herbert D. 1955 In Methods in Enzymology 1 p. 753 Colowick S. P., Kaplan N. O. Ed. New York: Academic Press Inc.;
     [Google Scholar]
  11. Heyningen W.E.VAN, Gladstone G. P. 1958; The neurotoxin of Shigella shigae. 3. The effect of iron on production of the toxin. Brit. J. exp. Path 34:221
     [Google Scholar]
  12. Hodgkiss W., Liston J., Goodwin T. W., Jamikorn M. 1954; The isolation and description of two marine microorganisms with special reference to their pigment production. J. gen. Microbiol 11:438
     [Google Scholar]
  13. Jose A. G., Wilson P. W. 1959; Metabolic activities of subcellular particles from Azotobader vinelandii. . Proc. nat. Acad. Sci., Wash 45492
     [Google Scholar]
  14. Karlsson J. L., Barker H. A. 1948; Evidence against the occurrence of a tricarboxylic acid cycle in Azotobader agilis . J. biol. Chem 175:913
     [Google Scholar]
  15. Kaufman S. 1955 In Methods in Enzymology 1 p. 714 Colowick S. P., Kaplan N. O. Ed. New York: Academic Press Inc.;
     [Google Scholar]
  16. Knox R. 1953; The effect of temperature on enzymic adaptation, growth and drug resistance. In Adaptation in Microorganisms . Symp. Soc. gen. Microbiol 3:184
     [Google Scholar]
  17. Kogut M., Podoski E. P. 1953; Oxidative pathways in a fluorescent Pseudomonas . Biochem. J 55:800
     [Google Scholar]
  18. Krebs H. A., Gurin S., Eggleston L. Y. 1952; The pathway of oxidation of acetate in baker’s yeast. Biochem. J 51:614
     [Google Scholar]
  19. Linnane A. W., Still J. L. 1955; The intracellular distribution of enzymes in Serratia marcescens . Biochim. biophys. Acta 16:305
     [Google Scholar]
  20. Lipmann F., Tuttle L. C. 1950; Lipase-catalysed condensation of fatty acids with hydroxylamine. Biochim. biophys. Acta 4:301
     [Google Scholar]
  21. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the folin phenol reagent. J. biol. Chem 193:265
     [Google Scholar]
  22. Markert C. L., Møller F. 1959; Multiple forms of enzymes: Tissue, ontogenetic and species specific patterns. Proc. nat. Acad. Sci., Wash 45:753
     [Google Scholar]
  23. Mcquillen K. 1956; Capabilities of bacterial protoplasts. In Bacterial Anatomy. Symp. Soc. gen. Microbiol 6:127
     [Google Scholar]
  24. Mitchell P. 1949; A new technique for stirred aerated culture. Nature; Lond.: 164846
     [Google Scholar]
  25. Mitchell P. 1957; A general theory of membrane transport from studies of bacteria. Nature; Lond.: 180134
     [Google Scholar]
  26. Mitchell P. 1959; Structure and function in microorganisms. Biochem. Soc. Symp 16:73
     [Google Scholar]
  27. Mitchell P., Moyle J. 1956; Osmotic function and structure in bacteria. In Bacterial Anatomy. Symp. Soc. gen. Microbiol 6:150
     [Google Scholar]
  28. Mitchell P., Moyle J. 1959; Succinyl group-translocation through the plasma membrane of Micrococcus lysodeikticus . Biochem. J 72:21P.
     [Google Scholar]
  29. Monod J., Cohen-Bazire G., Cohn M. 1951; Sur la biosynthese de la β-galactosidase (lactase) chez Escherichia coli. La specificite de l’induction. Biochim. biophys. Acta 7:585
     [Google Scholar]
  30. Monod J., Pappenheimer A. M., Cohen-Bazire G. 1952; La cinetique de la biosynthese de la β-galactosidase chez Escherichia coli consideree comme fonction de la croissance. Biochim. biophys. Acta 9:648
     [Google Scholar]
  31. Moses V. 1955; Tricarboxylic acid cycle reactions in the fungus Zygorrhynchus moelleri . J. gen. Microbiol 13:235
     [Google Scholar]
  32. Neidhardt F. C., Magasanik B. 1957; Effect of mixtures of substrates on the biosynthesis of inducible enzymes in Aerobacter aerogenes . J. Bact 73:260
     [Google Scholar]
  33. Penrose M., Quastel J. H. 1930; Cell structure and cell activity. Proc. roy. Soc B 107168
     [Google Scholar]
  34. Rickenberg H. V. 1957; The site of galactoside-permease activity in Escherichia coli . Biochim. biophys. Acta 25:206
     [Google Scholar]
  35. Salton M. R. J. 1957; The properties of lysozyme and its action on microorganisms. Bact. Rev 21:82
     [Google Scholar]
  36. Singer T. P., Kearney E. B. 1957 In Methods of Biochemical Analysis iv p. 307 Glick D. Ed. New York: Interscience Publishers Inc.;
     [Google Scholar]
  37. Sistrom W. R. 1958; On the physical state of intracellularly accumulated substrates of ²-galactosidase-permease of Escherichia coli . Biochim. biophys. Acta 29:579
     [Google Scholar]
  38. Spiegelman S., Dunn R. 1947; Interactions between enzyme-forming systems during adaptation. J. gen. Physiol 31:153
     [Google Scholar]
  39. Stadtman E. R., Barker H. A. 1950; Fatty acid synthesis by enzyme preparations of Clostridium kluyveri. YI. Reactions of acyl phosphates. J. biol. Chem 184:769
     [Google Scholar]
  40. Stone R. W., Wilson P. W. 1952; Respiratory activity of cell-free extracts from azotobacter. J. Bact 63:605
     [Google Scholar]
  41. Storck R., Wachsman J. T. 1957; Enzyme localization in Bacillus megaterium. . J. Bact 73:784
     [Google Scholar]
  42. Weibull C. 1953; The isolation of protoplasts from Bacillus megaterium by controlled treatment with lysozyme. J. Bact 66:688
     [Google Scholar]
  43. Weibull C., Beckman H., Bergström L. 1959; Localization of enzymes in Bacillus megaterium, strain M. J. gen. Microbiol 20:519
     [Google Scholar]
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The Oxidation of Tricarboxylic Acid Cycle Intermediates by a Strain of Corynebacterium erythrogenes
Microbiology 23, 267 (1960); https://doi.org/10.1099/00221287-23-2-267
/content/journal/micro/10.1099/00221287-23-2-267
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