Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1974 Apr;118(1):32–40. doi: 10.1128/jb.118.1.32-40.1974

Inhibition of Thiamine Pyrophosphate Utilization by Thiamine or Its Monophosphate in Escherichia coli

Hideo Nakayama 1, Ryoji Hayashi 1
PMCID: PMC246636  PMID: 4595201

Abstract

The growth of a thiamine pyrophosphate auxotroph of Escherichi coli was inhibited by either thiamine or thiamine monophosphate, and the growth of a thiamine monophosphate auxotroph was inhibited by thiamine. The thiamine pyrophosphate-dependent oxidation of pyruvate was inhibited by thiamine with whole cells of the thiamine pyrophosphate auxotroph but not with cell extracts prepared from the same organism. In addition, the thiamine pyrophosphate uptake of the thiamine pyrophosphate auxotroph was inhibited by either thiamine or thiamine monophosphate. Although the thiamine pyrophosphate uptake of a revertant, selected for prototrophy from the thiamine monophosphate auxotroph, was inhibited by thiamine to an extent comparable to that observed with the thiamine monophosphate auxotroph, its growth was no longer inhibited by thiamine. A possible mechanism for the inhibition by thiamine and thiamine monophosphate in the utilization of thiamine pyrophosphate is discussed.

Full text

PDF
32

Selected References

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

  1. Buchman E. R., Heegaard E., Bonner J. Inhibition of Carboxylase by Thiazole Pyrophosphate. Proc Natl Acad Sci U S A. 1940 Sep 15;26(9):561–563. doi: 10.1073/pnas.26.9.561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. GOUNARIS A. D., HAGER L. P. A resolution of the Escherichia coli pyruvate dehydrogenase complex. J Biol Chem. 1961 Apr;236:1013–1018. [PubMed] [Google Scholar]
  4. Iwashima A., Matsuura A., Nose Y. Thiamine-binding protein of Escherichia coli. J Bacteriol. 1971 Dec;108(3):1419–1421. doi: 10.1128/jb.108.3.1419-1421.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kawasaki T., Esaki K. Thiamine uptake in Escherichia coli. 3. Regulation of thiamine uptake in Escherichia coli. Arch Biochem Biophys. 1971 Jan;142(1):163–169. doi: 10.1016/0003-9861(71)90271-2. [DOI] [PubMed] [Google Scholar]
  6. Kawasaki T., Miyata I., Esaki K., Nose Y. Thiamine uptake in Escherichia coli. I. General properties of thiamine uptake system in Escherichia coli. Arch Biochem Biophys. 1969 Apr;131(1):223–230. doi: 10.1016/0003-9861(69)90125-8. [DOI] [PubMed] [Google Scholar]
  7. Matsuura A., Iwashima A., Nose Y. Inhibition by thiamine phosphates of thiamine uptake in Escherichia coli. J Vitaminol (Kyoto) 1972 Mar 10;18(1):29–33. doi: 10.5925/jnsv1954.18.29. [DOI] [PubMed] [Google Scholar]
  8. Morey A. V., Juni E. Studies on the nature of the binding of thiamine pyrophosphate to enzymes. J Biol Chem. 1968 Jun 10;243(11):3009–3019. [PubMed] [Google Scholar]
  9. NAVAZIO F., SILIPRANDI N., ROSSIFANELLI A. Pure crystalline oxythiamine phosphoric esters; preparation and some chemical and biological properties. Biochim Biophys Acta. 1956 Feb;19(2):274–279. doi: 10.1016/0006-3002(56)90428-0. [DOI] [PubMed] [Google Scholar]
  10. Nakayama H., Hayashi R. Biosynthesis of thiamine pyrophosphate in Escherichia coli. J Bacteriol. 1972 Feb;109(2):936–938. doi: 10.1128/jb.109.2.936-938.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Nakayama H., Hayashi R. Biosynthetic pathway of thiamine pyrophosphate: a special reference to the thiamine monophosphate-requiring mutant and the thiamine pyrophosphate-requiring mutant of Escherichia coli. J Bacteriol. 1972 Dec;112(3):1118–1126. doi: 10.1128/jb.112.3.1118-1126.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Nishimune T., Hayashi R. Thiamine-binding protein and thiamine uptake by Escherichia coli. Biochim Biophys Acta. 1971 Sep 21;244(3):573–583. doi: 10.1016/0304-4165(71)90074-2. [DOI] [PubMed] [Google Scholar]
  13. VELLUZ L., HERBAIN M. Oxythiamine triphosphoric acid; an effective inhibitor of the carboxylase system. J Biol Chem. 1951 May;190(1):241–244. [PubMed] [Google Scholar]
  14. WOOLLEY D. W. An enzymatic study of the mode of action of pyrithiamine (neopyrithiamine). J Biol Chem. 1951 Jul;191(1):43–54. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES