Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Dec;68(12):2903–2907. doi: 10.1073/pnas.68.12.2903

Vitamin B6-Responsive Histidine Deficiency in Mutants of Salmonella typhimurium

Gary B Henderson 1, Esmond E Snell 1
PMCID: PMC389556  PMID: 4943547

Abstract

A mutant of Salmonella typhimurium LT-2 that requires either vitamin B6 or histidine for growth was found to synthesize vitamin B5 in amounts comparable to the parent strain, but to be deficient in imidazoleacetol phosphate transaminase (L-histidinolphosphate: 2-oxoglutarate aminotransferase, EC 2.6.1.9), an enzyme required for histidine biosynthesis. The mutant apotransaminase required a 50-fold higher concentration of pyridoxal 5′-phosphate for half-maximum activation than the corresponding wild-type enzyme; the fully activated mutant enzyme also displays a much lower maximum rate of catalysis than the enzyme from the parent strain. Such mutational changes in bacteria resemble those in certain vitamin B6-responsive genetic diseases in man and provide useful experimental material for the study of factors involved in coenzyme binding and enzymatic catalysis.

Keywords: pyridoxal, imidazoleacetol phosphate transaminase, cofactor binding, enzyme stability, histidinolphosphatase

Full text

PDF
2903

Images in this article

2904Image
on p.2904
2904Image
on p.2904

Selected References

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

  1. AMES B. N., GARRY B., HERZENBERG L. A. The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1960 Apr;22:369–378. doi: 10.1099/00221287-22-2-369. [DOI] [PubMed] [Google Scholar]
  2. AMES B. N., HORECKER B. L. The biosynthesis of histidine: imidazoleacetol phosphate transaminase. J Biol Chem. 1956 May;220(1):113–128. [PubMed] [Google Scholar]
  3. Dempsey W. B., Ito H. Characterization of pyridoxine auxotrophs of Escherichia coli: serine and pdxF mutants. J Bacteriol. 1970 Nov;104(2):658–667. doi: 10.1128/jb.104.2.658-667.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Eberle H., Masker W. Effect of nalidixic acid on semionservative replication and repair synthesis after ultraviolet irradiation in Escherichia coli. J Bacteriol. 1971 Mar;105(3):908–912. doi: 10.1128/jb.105.3.908-912.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Frimpter G. W., Andelman R. J., George W. F. Vitamin B6-dependency syndromes. New horizons in nutrition. Am J Clin Nutr. 1969 Jun;22(6):794–805. doi: 10.1093/ajcn/22.6.794. [DOI] [PubMed] [Google Scholar]
  6. Grimminger H., Lingens F. Alternate requirement for pyridoxine or isoleucine in mutants of Escherichia coli. FEBS Lett. 1969 Nov 12;5(3):225–226. doi: 10.1016/0014-5793(69)80338-8. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Martin R. G., Goldberger R. F. Imidazolylacetolphosphate:L-glutamate aminotransferase. Purification and physical properties. J Biol Chem. 1967 Mar 25;242(6):1168–1174. [PubMed] [Google Scholar]
  9. Mudd S. H. Pyridoxine-responsive genetic disease. Fed Proc. 1971 May-Jun;30(3):970–976. [PubMed] [Google Scholar]
  10. Scriver C. R. Vitamin B6 deficiency and dependency in man. Am J Dis Child. 1967 Jan;113(1):109–114. doi: 10.1001/archpedi.1967.02090160159025. [DOI] [PubMed] [Google Scholar]
  11. Snell E. E. Analogs of pyridoxal or pyridoxal phosphate: relation of structure to binding with apoenzymes and to catalytic activity. Vitam Horm. 1970;28:265–290. doi: 10.1016/s0083-6729(08)60897-3. [DOI] [PubMed] [Google Scholar]
  12. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  13. Voll M. J. Translation and polarity in the histidine operon. 3. The isolation of prototrophic polar mutations. J Mol Biol. 1967 Nov 28;30(1):109–124. doi: 10.1016/0022-2836(67)90247-1. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES