1887

Abstract

Histidinol dehydrogenase has been purified from a derepressed mutant of B. A molecular weight of about 91000 was estimated by gel filtration. The native enzyme seems to be composed of two similar subunits which have a molecular weight of 52000 as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The pI of the enzyme as determined by isoelectric focusing is 4·75. The enzyme is maximally active at pH 9·5. It is highly specific for NAD and histidinol, with a (NAD) of 0.57 mM and a (histidinol) of 14 m. Mn is required for maximal activity. The enzyme is completely inactivated by 8 -urea but regains its activity very quickly upon removal of the urea. Mn and histidinol protect the enzyme from heat inactivation.

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/content/journal/micro/10.1099/00221287-128-3-579
1982-03-01
2021-05-15
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References

  1. Andrews P. 1965; The gel filtration behaviour of proteins related to their molecular weights over a wide range. Biochemical Journal 96:595–606
    [Google Scholar]
  2. Bitar K. G., Firca J. R., Loper J. C. 1977; Histidinol dehydrogenase from Salmonella typhi-murium and Escherichia coli. . Biochimica et biophysica acta 493:429–440
    [Google Scholar]
  3. Davis B. D., Mingioli E. V. 1950; Mutants of Escherichia coli requiring methionine or vitamin B12. Journal of Bacteriology 62:17–28
    [Google Scholar]
  4. Dhawale M. R., Creaser E. H., Loper J. C. 1972; Evolutionary mechanism of adaptation of Arthrobacter histidinolovorans and Pseudomonas aeruginosa to use l-histidinol as a sole source of nitrogen and carbon. Journal of General Microbiology 73:353–358
    [Google Scholar]
  5. Garrick-Silversmith L., Hartman P. E. 1970; Histidine-requiring mutants of Escherichia coli K12. Genetics 66:231–244
    [Google Scholar]
  6. Goldschmidt E. P., Cater M. S. 1970; Genetic analysis of histidine operon in Escherichia coli K12. Genetics 66:219–229
    [Google Scholar]
  7. Greeb J., Atkins J. F., Loper J. C. 1971; Histidinol dehydrogenase (hisD) mutants of Salmonella typhimurium. . Journal of Bacteriology 106:421–431
    [Google Scholar]
  8. Jaenicke R. J., Rudolf R., Heider I. 1979; Quaternary structure, subunits activity, and in vitro association of porcine mitochondrial malic dehydrogenase. Biochemistry 18:1217–1223
    [Google Scholar]
  9. Keesey J. K., Bigelis R., Fink G. R. 1979; The product of his 4 gene cluster in Saccharomyces cerevisiae. . Journal of Biological Chemistry 254:7427–7433
    [Google Scholar]
  10. Lindsay J. A., Creaser E. H. 1977; Purification and properties of histidinol dehydrogenase from psychrophilic, mesophilic and thermophilic bacilli. Biochemical Journal 165:247–253
    [Google Scholar]
  11. Loper J. C. 1968; Histidinol dehydrogenase from Salmonella typhimurium. . Journal of Biological Chemistry 243:3264–3272
    [Google Scholar]
  12. Marangos P. J., Constantinides S. M. 1974; Factors affecting the folding and association of flounder muscle glyceraldehyde-3-phosphate dehydrogenase in vitro. . Biochemistry 13:904–914
    [Google Scholar]
  13. Minson A. C., Creaser E. H. 1969; Purification of a trifunctional enzyme, catalysing three steps of the histidine pathway, from Neurospora crassa. . Biochemical Journal 114:49–56
    [Google Scholar]
  14. Roth J. R., Anton D. N., Hartman P. E. 1966; Histidine regulatory mutants in Salmonella typhimurium. . Journal of Molecular Biology 22:305–323
    [Google Scholar]
  15. Vesterberg O. 1972; Isoelectric focusing of proteins in polyacrylamide gels. Biochimica et biophysica acta 257:11–19
    [Google Scholar]
  16. Weber K., Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulphate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]
  17. Yamato S., Murachi T. 1979; Dissociation and association of fumarase subunits with special reference to the formation of dehydrogenase from Salmonella typhimurium. . European Journal of Biochemistry 93:189–195
    [Google Scholar]
  18. Yourno J. 1968; Composition and subunit structure of histidinol dehydrogenase from Salmonella typhimurium. . Journal of Biological Chemistry 243:3277–3288
    [Google Scholar]
  19. Yourno J., Ino I. 1968; Purification and crystalization of histidinol dehydrogenase from Salmonella typhimurium LT-2. Journal of Biological Chemistry 243:3273–3276
    [Google Scholar]
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