Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1969 Aug;114(1):49–56. doi: 10.1042/bj1140049

Purification of a trifunctional enzyme, catalysing three steps of the histidine pathway, from Neurospora crassa

A C Minson 1, E H Creaser 1
PMCID: PMC1184794  PMID: 4309307

Abstract

1. A procedure is described for the purification of an enzyme from Neurospora crassa that has three catalytic functions. These are 1-N-(5′-phosphoribosyl)-ATP pyrophosphohydrolase, 1-N-(5′-phosphoribosyl)-AMP cyclohydrolase and histidinol dehydrogenase (l-histidinol–NAD oxidoreductase, EC 1.1.1.23), and are responsible for the catalysis of reactions 2, 3 and 10 in the histidine pathway. The ratio of these three catalytic activities remains approximately the same throughout the purification procedure. Evidence is presented that the purified preparations contain a single protein exhibiting association–dissociation equilibria.

Full text

PDF
49

Selected References

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

  1. AHMED A., CASE M. E., GILES N. H. THE NATURE OF COMPLEMENTATION AMONG MUTANTS IN THE HISTIDINE-3 REGION OF NEUROSPORA CRASSA. Brookhaven Symp Biol. 1964 Dec;17:53–65. [PubMed] [Google Scholar]
  2. 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]
  3. 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]
  4. Ahmed A. Organization of the histidine-3 region of Neurospora. Mol Gen Genet. 1968;103(2):185–193. doi: 10.1007/BF00427145. [DOI] [PubMed] [Google Scholar]
  5. Bennett D. J., Creaser E. H. Amino acid substitutions in mutant forms of histidinol dehydrogenase from Neurospora crassa. Biochem J. 1967 Oct;105(1):39–44. doi: 10.1042/bj1050039. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Berlyn M. B. Gene-enzyme relationships in histidine biosynthesis in Aspergillus nidulans. Genetics. 1967 Nov;57(3):561–570. doi: 10.1093/genetics/57.3.561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Creaser E. H., Bennett D. J., Drysdale R. B. Studies on biosynthetic enzymes. I. Mutant forms of histidinol dehydrogenase from Neurospora crassa. Can J Biochem. 1965 Jul;43(7):993–1000. doi: 10.1139/o65-112. [DOI] [PubMed] [Google Scholar]
  8. Creaser E. H., Bennett D. J., Drysdale R. B. The purification and properties of histidinol dehydrogenase from Neurospora crassa. Biochem J. 1967 Apr;103(1):36–41. doi: 10.1042/bj1030036. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fink G. R. A cluster of genes controlling three enzymes in histidine biosynthesis in Saccharomyces cerevisiae. Genetics. 1966 Mar;53(3):445–459. doi: 10.1093/genetics/53.3.445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fink G. R. A cluster of genes controlling three enzymes in histidine biosynthesis in Saccharomyces cerevisiae. Genetics. 1966 Mar;53(3):445–459. doi: 10.1093/genetics/53.3.445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
  12. 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]
  13. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  14. SMITH D. W., AMES B. N. INTERMEDIATES IN THE EARLY STEPS OF HISTIDINE BIOSYNTHESIS. J Biol Chem. 1964 Jun;239:1848–1855. [PubMed] [Google Scholar]
  15. SMITH D. W., AMES B. N. PHOSPHORIBOSYLADENOSINE MONOPHOSPHATE, AN INTERMEDIATE IN HISTIDINE BIOSYNTHESIS. J Biol Chem. 1965 Jul;240:3056–3063. [PubMed] [Google Scholar]
  16. SMITHIES O. Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem J. 1955 Dec;61(4):629–641. doi: 10.1042/bj0610629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. WHITFIELD H. J., Jr, SMITH D. W., MARTIN R. G. SEDIMENTATION PROPERTIES OF THE ENZYMES OF THE HISTIDINE OPERON. J Biol Chem. 1964 Oct;239:3288–3291. [PubMed] [Google Scholar]

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

RESOURCES