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

doi:10.1016/0005-2744(72)90352-X

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 journal › Article › peer-review

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 language	English
Pages (from-to)	550-561
Number of pages	12
Journal	BBA - Enzymology
Volume	268
Issue number	2
DOIs	https://doi.org/10.1016/0005-2744(72)90352-X
Publication status	Published - 12 May 1972
Externally published	Yes

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title = "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",

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.",

author = "Hoffmann, {P. J.} and Doy, {C. H.} and Catcheside, {D. E.A.}",

year = "1972",

month = may,

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doi = "10.1016/0005-2744(72)90352-X",

language = "English",

volume = "268",

pages = "550--561",

journal = "BBA - Enzymology",

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number = "2",

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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. / Hoffmann, P. J.; Doy, C. H.; Catcheside, D. E.A.
In: BBA - Enzymology, Vol. 268, No. 2, 12.05.1972, p. 550-561.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - 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

AU - Hoffmann, P. J.

AU - Doy, C. H.

AU - Catcheside, D. E.A.

PY - 1972/5/12

Y1 - 1972/5/12

N2 - 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.

AB - 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.

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JO - BBA - Enzymology

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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

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