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Chemical Compound Review

quinate     (3R,5R)-1,3,4,5- tetrahydroxycyclohexane-1...

Synonyms: Chinasaure, L-Quinate, PubChem8105, D-QUINIC ACID, L-Quinic acid, ...
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Disease relevance of quinic acid


High impact information on quinic acid

  • CGA acts as an antioxidant in plants and protects against degenerative, age-related diseases in animals when supplied in their diet. cDNA clones encoding the enzyme that synthesizes CGA, hydroxycinnamoyl-CoA quinate: hydroxycinnamoyl transferase (HQT), were characterized from tomato and tobacco [6].
  • Purification and characterization of hydroxycinnamoyl D-glucose. Quinate hydroxycinnamoyl transferase in the root of sweet potato, Ipomoea batatas Lam [7].
  • Mutations in the qutR gene alter QUTR function such that the transcription of the qut gene cluster is permanently on (constitutive phenotype) or is insensitive to the presence of quinate (super-repressed phenotype) [8].
  • At the usual in vitro growth pH of 6.5, quinate enters the mycelium by means of a specific permease and is converted into PCA by the sequential action of the enzymes quinate dehydrogenase, 3-dehydroquinase and DHS dehydratase [9].
  • Attempts to partially decouple quinate permease from the control over flux by measuring flux at pH 3.5 (when a significant percentage of the soluble quinate is protonated and able to enter the mycelium without the aid of a permease) led to an increase of approx. 50% in the flux control coefficient for dehydroquinase [9].

Chemical compound and disease context of quinic acid


Biological context of quinic acid

  • The qa-3 gene, one of the four genes in the qa gene cluster, encodes quinate (shikimate) dehydrogenase (quinate: NAD oxidoreductase, ER, the first enzyme in the inducible quinic acid catabolic pathway in Neurospora crassa [13].
  • Taken together with the fact that A. nidulans has a very efficient pH homeostasis mechanism, these experiments are consistent with the view that quinate permease exerts a high degree of control over pathway flux under the standard laboratory growth conditions at pH 6 [9].
  • The ability of relatively stable Cr(V) and Cr(IV) complexes with 2-hydroxycarboxylato ligands [2-ethyl-2-hydroxybutanoate(2-) = ehba; (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylate(2-) = quinate = qa] to induce single-strand breaks in plasmid DNA has been studied under a wide range of reaction conditions [14].
  • Here, the multiple-level regulation of expression of the pca-qui operon encoding the enzymes for protocatechuate and quinate degradation was studied [15].
  • Catabolism of quinate and skikimate is initiated by NAD(+)-dependent dehydrogenases in other microorganisms, so it is evident that different gene pools were called upon to provide the ancestral enzyme for this metabolic step [16].

Anatomical context of quinic acid


Associations of quinic acid with other chemical compounds


Gene context of quinic acid


Analytical, diagnostic and therapeutic context of quinic acid

  • The qutB gene of A. nidulans encoding quinate dehydrogenase has similarly been subjected to PCR amplification and expression in E. coli [28].
  • Northern blot and suppression subtractive hybridization analyses showed that presence of a low amount of quinate, inducer of the quinate pathway, resulted in increased levels of arom mRNA, consistent with the compensation effect observed in ascomycetes [29].


  1. Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli. Lindner, H.A., Nadeau, G., Matte, A., Michel, G., Ménard, R., Cygler, M. J. Biol. Chem. (2005) [Pubmed]
  2. Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus. Elsemore, D.A., Ornston, L.N. J. Bacteriol. (1995) [Pubmed]
  3. Catabolism of benzoate and monohydroxylated benzoates by Amycolatopsis and Streptomyces spp. Grund, E., Knorr, C., Eichenlaub, R. Appl. Environ. Microbiol. (1990) [Pubmed]
  4. Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein. van Kleef, M.A., Duine, J.A. Arch. Microbiol. (1988) [Pubmed]
  5. New developments in oxidative fermentation. Adachi, O., Moonmangmee, D., Toyama, H., Yamada, M., Shinagawa, E., Matsushita, K. Appl. Microbiol. Biotechnol. (2003) [Pubmed]
  6. Engineering plants with increased levels of the antioxidant chlorogenic acid. Niggeweg, R., Michael, A.J., Martin, C. Nat. Biotechnol. (2004) [Pubmed]
  7. Purification and characterization of hydroxycinnamoyl D-glucose. Quinate hydroxycinnamoyl transferase in the root of sweet potato, Ipomoea batatas Lam. Villegas, R.J., Kojima, M. J. Biol. Chem. (1986) [Pubmed]
  8. Identification of domains responsible for signal recognition and transduction within the QUTR transcription repressor protein. Levett, L.J., Si-Hoe, S.M., Liddle, S., Wheeler, K., Smith, D., Lamb, H.K., Newton, G.H., Coggins, J.R., Hawkins, A.R. Biochem. J. (2000) [Pubmed]
  9. Control of metabolic flux through the quinate pathway in Aspergillus nidulans. Wheeler, K.A., Lamb, H.K., Hawkins, A.R. Biochem. J. (1996) [Pubmed]
  10. Transcriptional organization of genes for protocatechuate and quinate degradation from Acinetobacter sp. strain ADP1. Dal, S., Trautwein, G., Gerischer, U. Appl. Environ. Microbiol. (2005) [Pubmed]
  11. A gene involved in quinate metabolism is specific to one DNA homology group of Xanthomonas campestris. Lee, Y.A., Lo, Y.C., Yu, P.P. J. Appl. Microbiol. (1999) [Pubmed]
  12. Utilization of quinate and p-hydroxybenzoate by actinomycetes: key enzymes and taxonomic relevance. Grund, E., Kutzner, H.J. J. Basic Microbiol. (1998) [Pubmed]
  13. Genetical and biochemical characterization of QA-3 mutants and revertants in the QA gene cluster of Neurospora crassa. Case, M.E., Pueyo, C., Barea, J.L., Giles, N.H. Genetics (1978) [Pubmed]
  14. In vitro plasmid DNA cleavage by chromium(V) and -(IV) 2-hydroxycarboxylato complexes. Levina, A., Barr-David, G., Codd, R., Lay, P.A., Dixon, N.E., Hammershøi, A., Hendry, P. Chem. Res. Toxicol. (1999) [Pubmed]
  15. Multiple-Level Regulation of Genes for Protocatechuate Degradation in Acinetobacter baylyi Includes Cross-Regulation. Siehler, S.Y., Dal, S., Fischer, R., Patz, P., Gerischer, U. Appl. Environ. Microbiol. (2007) [Pubmed]
  16. The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinate-shikimate dehydrogenase. Elsemore, D.A., Ornston, L.N. J. Bacteriol. (1994) [Pubmed]
  17. The physiological contribution of Acinetobacter PcaK, a transport system that acts upon protocatechuate, can be masked by the overlapping specificity of VanK. D'Argenio, D.A., Segura, A., Coco, W.M., Bünz, P.V., Ornston, L.N. J. Bacteriol. (1999) [Pubmed]
  18. Identification of an essential histidine residue at the active site of the tonoplast malate carrier in Catharanthus roseus cells. Dietz, K.J., Canut, H., Marigo, G. J. Membr. Biol. (1992) [Pubmed]
  19. 3-dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway. Adachi, O., Tanasupawat, S., Yoshihara, N., Toyama, H., Matsushita, K. Biosci. Biotechnol. Biochem. (2003) [Pubmed]
  20. High shikimate production from quinate with two enzymatic systems of acetic Acid bacteria. Adachi, O., Ano, Y., Toyama, H., Matsushita, K. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  21. Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M., Lapthorn, A.J. J. Biol. Chem. (2003) [Pubmed]
  22. PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter. Gerischer, U., Segura, A., Ornston, L.N. J. Bacteriol. (1998) [Pubmed]
  23. Genes for chlorogenate and hydroxycinnamate catabolism (hca) are linked to functionally related genes in the dca-pca-qui-pob-hca chromosomal cluster of Acinetobacter sp. strain ADP1. Smith, M.A., Weaver, V.B., Young, D.M., Ornston, L.N. Appl. Environ. Microbiol. (2003) [Pubmed]
  24. Enzymatic preparation of metabolic intermediates, 3-dehydroquinate and 3-dehydroshikimate, in the shikimate pathway. Adachi, O., Ano, Y., Toyama, H., Matsushita, K. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  25. Characterization of the 3-dehydroquinase domain of the pentafunctional AROM protein, and the quinate dehydrogenase from Aspergillus nidulans, and the overproduction of the type II 3-dehydroquinase from neurospora crassa. Hawkins, A.R., Moore, J.D., Adeokun, A.M. Biochem. J. (1993) [Pubmed]
  26. Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase. MacKintosh, C., Coggins, J., Cohen, P. Biochem. J. (1991) [Pubmed]
  27. Expression of the 3-phosphoglycerate kinase gene (pgkA) of Penicillium chrysogenum. Hoskins, I.C., Roberts, C.F. Mol. Gen. Genet. (1994) [Pubmed]
  28. Overproduction in Escherichia coli of the dehydroquinate synthase domain of the Aspergillus nidulans pentafunctional AROM protein. van den Hombergh, J.P., Moore, J.D., Charles, I.G., Hawkins, A.R. Biochem. J. (1992) [Pubmed]
  29. Characterization of the arom gene in Rhizoctonia solani, and transcription patterns under stable and induced hypovirulence conditions. Lakshman, D.K., Liu, C., Mishra, P.K., Tavantzis, S. Curr. Genet. (2006) [Pubmed]
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