Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1979 Sep 1;181(3):771–774. doi: 10.1042/bj1810771

The catalytically active form of histidinol dehydrogenase from Salmonella typhimurium.

E Bürger, H Görisch, F Lingens
PMCID: PMC1161219  PMID: 391222

Abstract

The active-enzyme-sedimentation procedure was used to identify the catalytically competent form of histidinol dehydrogenase (EC 1.1.1.23) isolated from Salmonella typhimurium. At pH 9.4 the active species has a sedimentation coefficient S20,W of 5.4S, indicating that the dimer with a mol.wt. of approx. 83 000 is the enzymically active form.

Full text

PDF
771

Selected References

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

  1. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bitar K. G., Firca J. R., Loper J. C. Histidinol dehydrogenase from salmonella typhimurium and Escherichia coli. Purification, some characteristics and the amino acid sequence around a reactive thiol group. Biochim Biophys Acta. 1977 Aug 23;493(2):429–440. doi: 10.1016/0005-2795(77)90199-4. [DOI] [PubMed] [Google Scholar]
  3. Cohen R., Mire M. Analytical-band centrifugation of an active enzyme-substrate complex. 1. Principle and practice of the centrifugation. Eur J Biochem. 1971 Nov 11;23(2):267–275. doi: 10.1111/j.1432-1033.1971.tb01618.x. [DOI] [PubMed] [Google Scholar]
  4. Greeb J., Atkins J. F., Loper J. C. Histidinol dehydrogenase (his D) mutants of Salmonella typhimurium. J Bacteriol. 1971 May;106(2):421–431. doi: 10.1128/jb.106.2.421-431.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kono T., Yourno J. Proteolytic release of a histidinol dehydrogenase fragment from the double enzyme histidinol dehydrogenase-imidazolylacetol-phosphate: L-glutamate aminotransferase. J Biol Chem. 1971 Apr 10;246(7):2203–2206. [PubMed] [Google Scholar]
  6. LOPER J. C., ADAMS E. PURIFICATION AND PROPERTIES OF HISTIDINOL DEHYDROGENASE FROM SALMONELLA TYPHIMURIUM. J Biol Chem. 1965 Feb;240:788–795. [PubMed] [Google Scholar]
  7. Loper J. C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. J Biol Chem. 1968 Jun 25;243(12):3264–3272. [PubMed] [Google Scholar]
  8. Pauly H. E., Pfleiderer G. D-glucose dehydrogenase from Bacillus megaterium M 1286: purification, properties and structure. Hoppe Seylers Z Physiol Chem. 1975 Oct;356(10):1613–1623. doi: 10.1515/bchm2.1975.356.2.1613. [DOI] [PubMed] [Google Scholar]
  9. Rechler M. M., Bruni C. B. Properties of a fused protein formed by genetic manipulation. Histidinol dehydrogenase-imidazolylacetol phosphate: L-glutamate aminotransferase. J Biol Chem. 1971 Mar 25;246(6):1806–1813. [PubMed] [Google Scholar]
  10. Roth J. R., Antón D. N., Hartman P. E. Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties. J Mol Biol. 1966 Dec 28;22(2):305–323. doi: 10.1016/0022-2836(66)90134-3. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  13. Yourno J. Composition and subunit structure of histidinol dehydrogenase from Salmonella typhimurium. J Biol Chem. 1968 Jun 25;243(12):3277–3288. [PubMed] [Google Scholar]
  14. Yourno J., Ino I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. J Biol Chem. 1968 Jun 25;243(12):3273–3276. [PubMed] [Google Scholar]
  15. Yourno J., Kohno T., Roth J. R. Enzyme evolution: generation of a bifunctional enzyme by fusion of adjacent genes. Nature. 1970 Nov 28;228(5274):820–824. doi: 10.1038/228820a0. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES