The separation of three allosterically inhibitable 3-deoxy-d-arabino-heptulosonate 7-phosphate synthases from extracts of Neurospora crassa and the purification of the tyrosine inhibitable isoenzyme

P. J. Hoffmann, C. H. Doy, D. E.A. Catcheside

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

1. 1. A method is described for the complete separation of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (7-phospho-2-keto-3-deoxy-d-arabino-heptonate d-erythrose-4-phosphate-lyase (pyruvate-phosphorylating), EC 4.1.2.15) isoenzymes inhibited by tryptophan (DAHP synthase (Trp)), phenylalanine (DAHP synthase (Phe)) and tyrosine (DAHP synthase (Tyr)). 2. 2. DAHP synthase (Tyr) is purified to homogeneity as judged by electrophoresis on polyacrylamide gels. The presence of the substrate phosphoenolpyruvate is necessary for stability during purification and subsequent storage. 3. 3. The purification procedure makes use of allosteric ligand dependent reversible changes of molecular weight. Purification by ligand-dependent changes of molecular weight may have wider applications.

Original languageEnglish
Pages (from-to)550-561
Number of pages12
JournalBBA - Enzymology
Volume268
Issue number2
DOIs
Publication statusPublished - 12 May 1972
Externally publishedYes

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