Comparative biogenetic anatomy of vitamin B1: A 13C NMR investigation of the biosynthesis of thiamin in Escherichia coli and in Saccharomyces cerevisiae

Journal of the American Chemical Society

Volumn 120, Issue 15, 1998, Pages 3581-3589

  Himmeldirk, Klaus ^a   Sayer, Brian G ^a   Spenser, Ian D ^a  

^a MCMASTER UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

THIAMINE;

ARTICLE; BIOSYNTHESIS; CARBON NUCLEAR MAGNETIC RESONANCE; ESCHERICHIA COLI; ISOTOPE LABELING; NONHUMAN; SACCHAROMYCES CEREVISIAE; VITAMIN METABOLISM;

ESCHERICHIA COLI; SACCHAROMYCES CEREVISIAE;

EID: 0032557233     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja973835r     Document Type: Article

References (50)

1. White, R. L.; Spenser, I. D. in Escherichia coli and Salmonella, Cellular and Molecular Biology, 2nd ed.; Neidhardt, F. C., Ed.; ASM Press: Washington, D.C., 1996; Vol. 1 pp 680-686.
2. Begley, T. P. Nat. Prod. Reps. 1996, 13, 177-185.
3. Estramareix, B.; David, S. New J. Chem. 1996, 20, 607-629.
4. Spenser, I. D.; White, R. L. Angew. Chem., Int. Ed. Engl. 1997, 36, 1032-1046.
5. See Jansen, B. C. P. In The Vitamins, Vol. 5, 2nd ed.; Sebrell, W. H., Harris, R. S. Eds.; Academic Press: New York 1972; pp 99-100.
6. 1 (Thiamin) and its Use in Medicine; MacMillan: New York, 1938.
7. Lohmann, K.; Schuster, P. Naturwissenschaften 1937, 25, 26-27.
8. Haj-Ahmad, Y.; Bilinski, C. A.; Russell, I.; Stewart, G. G. Can. J. Microbiol. 1992, 38, 1156-1161. We are informed by the authors that the quantities of thiamin content given in Tables 1-3 and referred to in the text of the paper as (mg/L) and (mg/g) are in fact (μg/L) and (μg/g).
9. Estramareix, B.; Lesieur, M. Biochim. Biophys. Acta 1969, 192, 375-377.
10. White, R. H.; Rudolph, F. B. Biochemistry 1979, 18, 2632-2636.
11. Estramareix, B. Biochim. Biophys. Acta 1970, 208, 170-171.
12. Linnett, P. E.; Walker, J. J. Chem. Soc. C 1967, 796-799.
13. Linnett, P. E.; Walker, J. Biochem. J. 1968, 109, 161-168.
14. White, R. L.; Spenser, I. D. Biochem. J. 1979, 179, 315-325.
15. Kumaoka, H.; Brown, G. M. Arch. Biochem. Biophys. 1967, 122, 378-384.
16. Yamada, K.; Morisaki, M.; Kumaoka, H. Biochim. Biophys. Acta 1983, 756, 41-48.
17. David, S.; Estramareix, B.; Hirshfeld, H. Biochim. Biophys. Acta 1967, 148, 11-21.
18. Uchida, K.; Yamada, K.; Kumaoka, H. Bitamin 1982, 56, 235-240.
19. Grue-Sørensen, G.; White, R. L.; Spenser, I. D. J. Am. Chem. Soc. 1986, 108, 146-158, 3863.
20. White, R. L.; Spenser, I. D. J. Am. Chem. Soc. 1979, 101, 5102-5104; 1982, 104, 4934-4943.
21. White, R. L.; Spenser, I. D. J. Am. Chem. Soc. 1979, 101, 5102-5104; 1982, 104, 4934-4943.
22. Yamada, K.; Yamamoto, M.; Hayashiji, M.; Tazuya, K.; Kumaoka, H. Biochem. Int. 1985, 10, 689-694.
23. White, R. H. Biochemistry 1978, 17, 3833-3840.
24. Thérisod, M.; Fischer, J.-C.; Estramareix, B. Biochem. Biophys. Res. Commun. 1981, 98, 374-379.
25. David, S.; Estramareix, B.; Fischer, J.-C.; Thérisod, M. J. Am. Chem. Soc. 1981, 103, 7341-7342.
26. David, S.; Estramareix, B.; Fischer, J.-C.; Thérisod, M. S. J. Chem. Soc., Perkin Trans. 1 1982, 2131-2137.
27. Yamada, K.; Kumaoka, H. Biochem. Int. 1982, 5, 771-776.
28. Yamada, K.; Kumaoka, H. J. Nutr. Sci. Vitaminol. 1983, 29, 389-398.
29. Newell, P. C.; Tucker, R. G. Biochem. J. 1968, 106, 279-287.
30. Estramareix, B.; Thérisod, M. J. Am. Chem. Soc. 1984, 106, 3857-3860.
31. Estramareix, M.; David, S. Biochem. Biophys. Res. Commun. 1986, 134, 1136-1141; Biochim. Biophys. Acta 1990, 1035, 154-160.
32. Estramareix, M.; David, S. Biochem. Biophys. Res. Commun. 1986, 134, 1136-1141; Biochim. Biophys. Acta 1990, 1035, 154-160.
33. Tazuya, K.; Morisaki, M.; Yamada, K.; Kumaoka, H.; Saiki, K. Biochem. Int. 1987, 14, 153-160.
34. Tazuya, K.; Tanaka, M.; Morisaki, M.; Yamada, K.; Kumaoka, H. Biochem. Int. 1987, 14, 769-777.
35. Horak, R. M.; Steyn, P. S.; Vleggar, R. Magn. Reson. Chem. 1985, 23, 995-1039.
36. Spenser, I. D.; Hill, R. E. Nat. Prod. Rep. 1995, 12, 555-565.
37. Tazuya, K.; Yamada, K.; Kumaoka, H. Biochim. Biophys. Acta 1989, 990, 73-79.
38. Himmeldirk, K.; Kennedy, I. A.; Hill, R. E.; Sayer, B. G.; Spenser, I. D. J. Chem. Soc., Chem. Commun. 1996, 1187-1188.
39. Breslow, R. J. Am. Chem. Soc. 1957, 79, 1762-1763.
40. 2O as the solvent was avoided in order to preclude deuterium/proton exchange at T-2, leading to multiplicity of the T-2 signal.
41. Kennedy, I. A.; Hemscheidt, T.; Britten, J. F.; Spenser, I. D. Can. J. Chem. 1995, 73, 1329-1337.
42. 41 but addition of L-threonine permits the mutant to grow.
43. Westley, J. W., Pruess, D. L.; Volpe, L. A.; Demny, T. C.; Stempel, A. J. Antibiot. 1971, 24, 330-1.
44. Olson, B. H.; Johnson, M. J. J. Bacteriol. 1949, 57, 235-246.
45. In experiments 2 and 4 L-asparagine was omitted from the medium.
46. 4 6.7 g/L.
47. Presumably as a result of a high degree of purification, the enzyme preparations sold by Fluka and by Sigma as Taka-Diastase did not show acid phosphatase activity. Such activity stems from a minor enzymic contaminant of the α-amylase enzyme preparation. The Fluka product, Claradiastase, showed phosphatase activity and can be used in place of the Sankyo product.
48. Gelotte, B. J. Chromatogr. 1960, 3, 330-342.
49. Davidek, J.; Pudil, F.; Seifert, J. J. Chromatogr. 1977, 140, 316-318.
50. 4 1 g/L.