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. 1975 Apr;122(1):215–223. doi: 10.1128/jb.122.1.215-223.1975

Regulation of the tricarboxylic acid cycle in gram-positive, facultatively anaerobic bacilli.

N Tanaka, R S Hanson
PMCID: PMC235660  PMID: 1123317

Abstract

The facultative anaerobes Bacillus polymyxa Hino G, B. polymyxa Hino J, and B.macerans were observed to have imcomplete tricarboxylic acid cycles. They were devoid of malate dehydrogenase and all had very low levels of alpha-ketoglutarate dehydrogenase. B. polymyxa Hino J was devoid of alpha-ketoglutarate dehydrogenase when grown aerobically and anerobically. Citrate synthase from B. polymyxa was inhibited by adenosine triphosphate but not reduced nicotinamide adenine dinucleotide and resembled enzymes from other gram-positive bacteria in this respect. Like the citrate synthases from gram-negative, facultative anaerobes and chemolithotrophs, the enzyme from B. polymyxa was inhibited by alpha-ketoglutarate. Inhibition by adenosine triphosphate was shown to be competitive with acetyl-coenzyme A and alpha-ketoglutarate inhibition was competitive with oxaloacetate.

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Selected References

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

  1. Amarasingham C. R., Davis B. D. Regulation of alpha-ketoglutarate dehydrogenase formation in Escherichia coli. J Biol Chem. 1965 Sep;240(9):3664–3668. [PubMed] [Google Scholar]
  2. Atkinson D. E. The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry. 1968 Nov;7(11):4030–4034. doi: 10.1021/bi00851a033. [DOI] [PubMed] [Google Scholar]
  3. Bulla L. A., St Julian G., Rhodes R. A., Hesseltine C. W. Physiology of sporeforming bacteria associated with insects. I. Glucose catabolism in vegetative cells. Can J Microbiol. 1970 Apr;16(4):243–248. doi: 10.1139/m70-045. [DOI] [PubMed] [Google Scholar]
  4. Carls R. A., Hanson R. S. Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis. J Bacteriol. 1971 Jun;106(3):848–855. doi: 10.1128/jb.106.3.848-855.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cox D. P., Hanson R. S. Catabolite repression of aconitate hydratase in Bacillus subtilis. Biochim Biophys Acta. 1968 Apr 16;158(1):36–44. doi: 10.1016/0304-4165(68)90069-x. [DOI] [PubMed] [Google Scholar]
  6. DAVIS B. D., GILVARG C. The role of the tricarboxylic acid cycle in acetate oxidation in Escherichia coli. J Biol Chem. 1956 Sep;222(1):307–319. [PubMed] [Google Scholar]
  7. DAVIS B. D. The teleonomic significance of biosynthetic control mechanisms. Cold Spring Harb Symp Quant Biol. 1961;26:1–10. doi: 10.1101/sqb.1961.026.01.005. [DOI] [PubMed] [Google Scholar]
  8. Davey J. F., Whittenbury R., Wilkinson J. F. The distribution in the methylobacteria of some key enzymes concerned with intermediary metabolism. Arch Mikrobiol. 1972;87(4):359–366. doi: 10.1007/BF00409135. [DOI] [PubMed] [Google Scholar]
  9. Flechtner V. R., Hanson R. S. Coarse and fine control of citrate synthase from Bacillus subtilis. Biochim Biophys Acta. 1969 Jul 30;184(2):252–262. doi: 10.1016/0304-4165(69)90027-0. [DOI] [PubMed] [Google Scholar]
  10. Flechtner V. R., Hanson R. S. Regulation of the tricarboxylic acid cycle in bacteria. A comparison of citrate synthases from different bacteria. Biochim Biophys Acta. 1970 Nov 24;222(2):253–264. doi: 10.1016/0304-4165(70)90114-5. [DOI] [PubMed] [Google Scholar]
  11. Fortnagel P., Freese E. Analysis of sporulation mutants. II. Mutants blocked in the citric acid cycle. J Bacteriol. 1968 Apr;95(4):1431–1438. doi: 10.1128/jb.95.4.1431-1438.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gray C. T., Wimpenny J. W., Mossman M. R. Regulation of metabolism in facultative bacteria. II. Effects of aerobiosis, anaerobiosis and nutrition on the formation of Krebs cycle enzymes in Escherichia coli. Biochim Biophys Acta. 1966 Mar 28;117(1):33–41. doi: 10.1016/0304-4165(66)90149-8. [DOI] [PubMed] [Google Scholar]
  13. HANSON H. M., WITOSLAWSKI J. J., CAMPBELL E. H. REVERSIBLE DISRUPTION OF A WAVELENGTH DISCRIMINATION IN PIGEONS FOLLOWING ADMINISTRATION OF PHENIPRAZINE. Toxicol Appl Pharmacol. 1964 Nov;6:690–695. doi: 10.1016/0041-008x(64)90119-x. [DOI] [PubMed] [Google Scholar]
  14. HANSON R. S., SRINIVASAN V. R., HALVORSON H. O. BIOCHEMISTRY OF SPORULATION. II. ENZYMATIC CHANGES DURING SPORULATION OF BACILLUS CEREUS. J Bacteriol. 1963 Jul;86:45–50. doi: 10.1128/jb.86.1.45-50.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. HINO S., WILSON P. W. Nitrogen fixation by a facultative bacillus. J Bacteriol. 1958 Apr;75(4):403–408. doi: 10.1128/jb.75.4.403-408.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hanson R. S., Cox D. P. Effect of different nutritional conditions on the synthesis of tricarboxylic acid cycle enzymes. J Bacteriol. 1967 Jun;93(6):1777–1787. doi: 10.1128/jb.93.6.1777-1787.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Johnson D. E., Hanson R. S. Bacterial citrate synthases: purification, molecular weight and kinetic mechanism. Biochim Biophys Acta. 1974 Jun 18;350(2):336–353. doi: 10.1016/0005-2744(74)90508-7. [DOI] [PubMed] [Google Scholar]
  18. Klofat W., Picciolo G., Chappelle E. W., Freese E. Production of adenosine triphosphate in normal cells and sporulation mutants of Bacillus subtilis. J Biol Chem. 1969 Jun 25;244(12):3270–3276. [PubMed] [Google Scholar]
  19. Klungsoyr L., Hagemen J. H., Fall L., Atkinson D. E. Interaction between energy charge and product feedback in the regulation of biosynthetic enzymes. Aspartokinase, phosphoribosyladenosine triphosphate synthetase, and phosphoribosyl pyrophosphate synthetase. Biochemistry. 1968 Nov;7(11):4035–4040. doi: 10.1021/bi00851a034. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. Matin A., Rittenberg S. C. Regulation of glucose metabolism in Thiobacillus intermedius. J Bacteriol. 1970 Oct;104(1):239–246. doi: 10.1128/jb.104.1.239-246.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Matin A., Rittenberg S. C. Regulation of glucose metabolism in Thiobacillus intermedius. J Bacteriol. 1970 Oct;104(1):239–246. doi: 10.1128/jb.104.1.239-246.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. NAKATA H. M., HALVORSON H. O. Biochemical changes occurring during growth and sporulation of Bacillus cereus. J Bacteriol. 1960 Dec;80:801–810. doi: 10.1128/jb.80.6.801-810.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Ouellette C. A., Burris R. H., Wilson P. W. Deoxyribonucleic acid base composition of species of Klebsiella, Azotobacter and Bacillus. Antonie Van Leeuwenhoek. 1969;35(3):275–286. doi: 10.1007/BF02219149. [DOI] [PubMed] [Google Scholar]
  25. Rutberg B., Hoch J. A. Citric acid cycle: gene-enzyme relationships in Bacillus subtilis. J Bacteriol. 1970 Nov;104(2):826–833. doi: 10.1128/jb.104.2.826-833.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Shen L. C., Fall L., Walton G. M., Atkinson D. E. Interaction between energy charge and metabolite modulation in the regulation of enzymes of amphibolic sequences. Phosphofructokinase and pyruvate dehydrogenase. Biochemistry. 1968 Nov;7(11):4041–4045. doi: 10.1021/bi00851a035. [DOI] [PubMed] [Google Scholar]
  27. Smith A. J., London J., Stanier R. Y. Biochemical basis of obligate autotrophy in blue-green algae and thiobacilli. J Bacteriol. 1967 Oct;94(4):972–983. doi: 10.1128/jb.94.4.972-983.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Srere P. A. The citrate enzymes: their structures, mechanisms, and biological functions. Curr Top Cell Regul. 1972;5:229–283. doi: 10.1016/b978-0-12-152805-8.50013-7. [DOI] [PubMed] [Google Scholar]
  29. Stern J. R., Bambers G. Glutamate biosynthesis in anaerobic bacteria. I. The citrate pathways of glutamate synthesis in Clostridium kluyveri. Biochemistry. 1966 Apr;5(4):1113–1118. doi: 10.1021/bi00868a001. [DOI] [PubMed] [Google Scholar]
  30. Taylor B. F., Hoare D. S. New facultative Thiobacillus and a reevaluation of the heterotrophic potential of Thiobacillus novellus. J Bacteriol. 1969 Oct;100(1):487–497. doi: 10.1128/jb.100.1.487-497.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Weitzman P. D., Dunmore P. Citrate synthases: allosteric regulation and molecular size. Biochim Biophys Acta. 1969 Jan 7;171(1):198–200. doi: 10.1016/0005-2744(69)90122-3. [DOI] [PubMed] [Google Scholar]
  32. Weitzman P. D.J., Dunmore P. Regulation of citrate synthase activity by alpha-ketoglutarate. Metabolic and taxonomic significance. FEBS Lett. 1969 Jun;3(4):265–267. doi: 10.1016/0014-5793(69)80154-7. [DOI] [PubMed] [Google Scholar]
  33. Weitzman P. D., Jones D. Regulation of citrate synthase and microbial taxonomy. Nature. 1968 Jul 20;219(5151):270–272. doi: 10.1038/219270a0. [DOI] [PubMed] [Google Scholar]
  34. Whitehead J. S., Kay E., Lew J. Y., Shannon L. M. A preparative column electrophoresis apparatus using Sephadex G-25. Anal Biochem. 1971 Apr;40(2):287–291. doi: 10.1016/0003-2697(71)90387-3. [DOI] [PubMed] [Google Scholar]
  35. Yousten A. A., Hanson R. S. Sporulation of tricarboxylic acid cycle mutants of Bacillus subtilis. J Bacteriol. 1972 Feb;109(2):886–894. doi: 10.1128/jb.109.2.886-894.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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