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Mise en évidence et propriétés de deux formes de la 5-déshydroquinate hydro-lyase chez les végétaux supérieurs

Characterization and properties of two dehydroquinate hydro-lyases in higher plants

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Summary

Two dehydroquinate hydro-lyases (E.C. 4.2.1.10) have been routinely separated from different organs of Zea mays L. by chromatography on Cellex-D Bio-Rad or hydroxypatite using linear salt gradients. Dehydroquinate hydro-lyase 1 is associated with shikimate: NADP+ oxidoreductase (E.C. 1.1.1.25). DHQase 2 is a free constitutive enzyme; in this respect it differs from the inducible enzyme of microorganisms which appears only when dehydroquinate or quinate is the principal carbon source. DHQase 1 and DHQase 2 have a similar apparent Michaelis constant and pH optimum, but they differ in their molecular weight, thermal stability and sensitivity to metabolic effectors. DHQase 2 is specifically activated by shikimic acid. This strong activation and the channeling properties of the complex involved in the shikimate pathway can provide an effective means of control in the utilization of dehydroquinate between two different pathways. The significance of such a system involving both a specific regulation of isoenzymes and a molecular compartmentation by means of an enzymatic complex is discussed.

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Abbreviations

DHQase:

5-déshydroquinate hydro-lyase

SH. ORase:

Shikimate: NADP+ oxydoréductase

5-DHS:

Acide 5-déshydroshikimique

5-DHQ:

Acide 5-déshydroquinique

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Authors and Affiliations

  1. Enzymologie et Métabolisme, Equipe de Recherche associée au CNRS, Université Paul Sabatier-Centre de Physiologie Végétale, 118, route de Narbonne, F-31077, Toulase Cédex, France

    Alain M. Boudet, Raymond Lécussan & Annie Boudet

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  1. Alain M. Boudet
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  2. Raymond Lécussan
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  3. Annie Boudet
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Boudet, A.M., Lécussan, R. & Boudet, A. Mise en évidence et propriétés de deux formes de la 5-déshydroquinate hydro-lyase chez les végétaux supérieurs. Planta 124, 67–75 (1975). https://doi.org/10.1007/BF00390069

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