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Chemical Compound Review:

KST-1A3888 (6R)-4- (dihydroxymethylidene)-2,6...

Synonyms:

Adachi, O. et al., Yi, J. et al., Schmitz, M. et al., Adachi, O. et al., Li, W. et al., et al.

Adachi, Ano, Toyama, Matsushita, Adachi, Ano, Toyama, Matsushita,

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Disease relevance of 3-dehydroshikimic acid

3-Dehydroquinate and 3-dehydroshikimate synthesized, respectively, by E. coli QP1.1/pJY1.216A and E. coli KL3/pJY1.216A from glucose were extracted and then reacted in water heated at 290 degrees C to afford catechol in overall yields from glucose of 10% and 26%, respectively [1].

High impact information on 3-dehydroshikimic acid

As part of continuing genetic and biochemical studies concerning the organization and regulation of this gene cluster, 3-dehydroshikimate dehydratase has been purified and characterized biochemically [2].
A deep pocket with a narrow entrance between the two domains, containing strictly conserved residues primarily contributed by the catalytic domain, is identified as a potential 3-dehydroshikimate binding pocket [3].
The enzyme 3-dehydroquinase catalyzes the interconversion of 3-dehydroquinate and 3-dehydroshikimate [4].
Antioxidant activity of 3-dehydroshikimic acid in liposomes, emulsions, and bulk oil [5].
Using a 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP, aroB(-))-producing strain, a fed-batch fermentation strategy specialized for glucose pulse experiments was developed and further applied for 3-dehydroshikimate (DHS, aroE(-))- and shikimate 3-phosphate (S3P, aroA(-))-producing E. coli strains [6].

Biological context of 3-dehydroshikimic acid

Escherichia coli KL3/pJY1.216A was cultured under fed-batch fermentor conditions where glucose was the only source of carbon for the formation of microbial biomass and the synthesis of product 3-dehydroshikimic acid [7].

Anatomical context of 3-dehydroshikimic acid

3-Dehydroquinate was further converted to 3-dehydroshikimate with a reasonable yield by growing cells and also immobilized cells [8].
3-Dehydroshikimate was formed with a yield of 57-77% from quinate via 3-dehydroquinate by two successive enzyme reactions, quinoprotein quinate dehydrogenase (QDH) and 3-dehydroquinate dehydratase, in the cytoplasmic membranes of acetic acid bacteria [9].

Associations of 3-dehydroshikimic acid with other chemical compounds

An optimal expression level of phosphoenolpyruvate synthase was identified, which did not correspond to the highest expression levels of this enzyme, where the total yield of 3-dehydroshikimic acid and shikimate pathway byproducts synthesized from glucose was 51% (mol/mol) [7].
The optimum pH for shikimate oxidation and 3-dehydroshikimate reduction was found at pH 10 and 7 respectively [10].

Analytical, diagnostic and therapeutic context of 3-dehydroshikimic acid

Sequence analysis and structural comparison led us to propose the catalytic machinery and a model for 3-dehydroshikimate recognition [11].

References

Benzene-free synthesis of catechol: interfacing microbial and chemical catalysis. Li, W., Xie, D., Frost, J.W. J. Am. Chem. Soc. (2005) [Pubmed]
Purification and characterization of 3-dehydroshikimate dehydratase, an enzyme in the inducible quinic acid catabolic pathway of Neurospora crassa. Strøman, P., Reinert, W.R., Giles, N.H. J. Biol. Chem. (1978) [Pubmed]
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. Ye, S., Von Delft, F., Brooun, A., Knuth, M.W., Swanson, R.V., McRee, D.E. J. Bacteriol. (2003) [Pubmed]
Crystallization and preliminary X-ray crystallographic analysis of type II dehydroquinase from Helicobacter pylori. Kwak , J.E., Lee , J.Y., Han , B.W., Moon J, J., Sohn , S.H., Suh , S.W. Acta Crystallogr. D Biol. Crystallogr. (2001) [Pubmed]
Antioxidant activity of 3-dehydroshikimic acid in liposomes, emulsions, and bulk oil. Chang, Y.C., Almy, E.A., Blamer, G.A., Gray, J.I., Frost, J.W., Strasburg, G.M. J. Agric. Food Chem. (2003) [Pubmed]
Pulse experiments as a prerequisite for the quantification of in vivo enzyme kinetics in aromatic amino acid pathway of Escherichia coli. Schmitz, M., Hirsch, E., Bongaerts, J., Takors, R. Biotechnol. Prog. (2002) [Pubmed]
Modulation of phosphoenolpyruvate synthase expression increases shikimate pathway product yields in E. coli. Yi, J., Li, K., Draths, K.M., Frost, J.W. Biotechnol. Prog. (2002) [Pubmed]
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]
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]
Purification and Properties of NADP-Dependent Shikimate Dehydrogenase from Gluconobacter oxydans IFO 3244 and Its Application to Enzymatic Shikimate Production. Adachi, O., Ano, Y., Toyama, H., Matsushita, K. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
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]

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