Purification of a trifunctional enzyme, catalysing three steps of the histidine pathway, from Neurospora crassa
- 1 August 1969
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 114 (1) , 49-56
- https://doi.org/10.1042/bj1140049
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.Keywords
This publication has 15 references indexed in Scilit:
- ACETYLORNITHINASE OF ESCHERICHIA COLI: PARTIAL PURIFICATION AND SOME PROPERTIESPublished by Elsevier ,2021
- Organization of the Histidine-3 region of NeurosporaMolecular Genetics and Genomics, 1968
- Amino acid substitutions in mutant forms of histidinol dehydrogenase from Neurospora crassaBiochemical Journal, 1967
- The purification and properties of histidinol dehydrogenase from Neurospora crassaBiochemical Journal, 1967
- STUDIES ON BIOSYNTHETIC ENZYMES: I. MUTANT FORMS OF HISTIDINOL DEHYDROGENASE FROM NEUROSPORA CRASSACanadian Journal of Biochemistry, 1965
- THE NATURE OF COMPLEMENTATION AMONG MUTANTS IN THE HISTIDINE-3 REGION OF NEUROSPORA CRASSA.1964
- Sedimentation Properties of the Enzymes of the Histidine OperonJournal of Biological Chemistry, 1964
- Intermediates in the Early Steps of Histidine BiosynthesisJournal of Biological Chemistry, 1964
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961
- THE BIOSYNTHESIS OF HISTIDINE: IMIDAZOLEACETOL PHOSPHATE TRANSAMINASEJournal of Biological Chemistry, 1956