[Characterization and Properties of Two Dehydroquinate Hydro-lyases in Higher Plants]

Overview

Journal Planta

Specialty Biology

Date 2014 Jan 18

PMID 24435175

Citations 1

Authors

A M Boudet

R Lecussan

A Boudet

Affiliations

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Abstract

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.

Citing Articles

Purification and properties of 5-enolpyruvylshikimate 3-phosphate synthase from seedlings of Pisum sativum L.

Mousdale D, Coggins J Planta. 2013; 160(1):78-83.

PMID: 24258375 DOI: 10.1007/BF00392469.

References

Stadtman E . The role of multiple enzymes in the regulation of branched metabolic pathways. Ann N Y Acad Sci. 1968; 151(1):516-30. DOI: 10.1111/j.1749-6632.1968.tb11911.x. View

Alibert G, Ranjeva R, Boudet A . [Studies on enzymes catalyzing phenolic acids formation in Quercus penduculata (Ehrh.). II. Intracellular location of phenylalanine ammonia-lyase, cinnamate 4-hydroxylase and "benzoate synthase"]. Biochim Biophys Acta. 1972; 279(2):282-9. View

Boudet A, Lecussan R . [Studies on the association of 5-dehydroquinate hydro-lyase and shikimate: NADP(+)-oxidoreductase in higher plants]. Planta. 2014; 119(1):71-9. DOI: 10.1007/BF00390823. View

Berlyn M, Ahmed S, GILES N . Organization of polyaromatic biosynthetic enzymes in a variety of photosynthetic organisms. J Bacteriol. 1970; 104(2):768-74. PMC: 285056. DOI: 10.1128/jb.104.2.768-774.1970. View

Lue P, Kaplan J . Metabolic compartmentation at the molecular level: the function of a multienzyme aggregate in the pyrimidine pathway of yeast. Biochim Biophys Acta. 1970; 220(3):365-72. DOI: 10.1016/0005-2744(70)90268-8. View

Lingens F, Goebel W, Uesseler H . [Regulation of biosynthesis of aromatic amino acids by Calviceps paspali]. Eur J Biochem. 1967; 2(4):442-7. DOI: 10.1111/j.1432-1033.1967.tb00157.x. View

Boudet A . . FEBS Lett. 1971; 14(4):257-261. DOI: 10.1016/0014-5793(71)80631-2. View

GILES N, Partridge C, Ahmed S, Case M . The occurrence of two dehydroquinases in Neurospora crassa, one constitutive and one inducible. Proc Natl Acad Sci U S A. 1967; 58(5):1930-7. PMC: 223886. DOI: 10.1073/pnas.58.5.1930. View

Lue P, Kaplan J . Aggregation states of a regulatory enzyme complex catalyzing the early steps of pyrimidine biosynthesis in bakers' yeast. Can J Biochem. 1971; 49(4):403-11. DOI: 10.1139/o71-059. View

10.

BALINSKY D, Davies D . Aromatic biosynthesis in higher plants. 3. Preparation and properties of dehydroquinase. Biochem J. 1961; 80:300-4. PMC: 1243998. DOI: 10.1042/bj0800300. View

11.

Cain R . Metabolism of shikimate and quinate by Aspergillus niger and its regulation. Biochem J. 1972; 127(2):15P-16P. PMC: 1178628. View

12.

Gibson F, Pittard J . Pathways of biosynthesis of aromatic amino acids and vitamins and their control in microorganisms. Bacteriol Rev. 1968; 32(4 Pt 2):465-92. PMC: 413161. View

13.

Ahmed S, GILES N . Organization of enzymes in the common aromatic synthetic pathway: evidence for aggregation in fungi. J Bacteriol. 1969; 99(1):231-7. PMC: 249992. DOI: 10.1128/jb.99.1.231-237.1969. View