Quinate

The constitution of laudanosine was determined by Pictet and Athanasescu/ who prepared it by reducing papaverine methochloride with tin and hydrochloric acid and deracemising the dZ-laudanosine (iV-methyltetrahydropapaverine) so obtained, by fractional crystallisation of the quinate. Laudanosine must, therefore, be represented by formula... 

Aligned sequences of 16 members of the sugar transporter family. Residues which are identical in 5=50% of the 16 sugar-transporter sequences (excluding the quinate transporter (qa-y), the citrate transporter (CIT), the tetracycline transporter (pBR322) and lac permease (LacY)) are highlighted, and recorded below the sequences as CONSERVED . The locations of predicted membrane-spanning helices are indicated by horizontal bars. The sequences were taken from the references cited in the text. 

The enhanced reactivity of the axial 5-hydroxyl group over that of the equatorial group on C-3 in methyl quinate towards acid chlorides in pyridine has been attributed147 to intramolecular hydrogenbonding of the former group to the syn-axially disposed oxygen atom on C-l. 

Figure 3. Hypothetical alternative enzyme path between 3-dehydroquinate and shikimate. A reversed order of the dehydratase and dehydrogenase steps of the classical pathway (top) would produce the quinate route (bottom).

Chlorogenate Chlorogenate 3,5-Dicaffeoyl-quinate (Isoch lorogenate) 59,60... 

With M. gryphiswaldense, Schuler and Bauerlein (1996) recorded an Fe uptake rate from Fe " citrate of 0.86 nmol min mg dry weight and suggested that the major portion of Fe is taken up in an energy-dependent process possibly by a reductive step (Schuler, 1999). Fukumori et al. (1997) proposed that the dissimilatory nitrite reductase of M. magnetotacticum may function as an Fe" oxidizing enzyme. Later, Fuko-mori (2000) suggested an Fe "quinate complex as the source of Fe which is subsequently reduced in the cell in a microaerobic environment at about neutral pH by the iron reductase NADH (an assimilatory enzyme). 

All carbons are derived from either erythrose 4-phosphate (light purple) or phosphoenolpyruvate (pink). Note that the NAD+ required as a cofactor in step (3) is released unchanged it may be transiently reduced to NADH during the reaction, with formation of an oxidized reaction intermediate. Step (6) is competitively inhibited by glyphosate (COO—CH2—NH—CH2—PO ), the active ingredient in the widely used herbicide Roundup. The herbicide is relatively nontoxic to mammals, which lack this biosynthetic pathway. The chemical names quinate, shikimate, and chorismate are derived from the names of plants in which these intermediates have been found to accumulate. 

Figure 26-7 Anion separation by ion chromatography with a gradient of electrolytically generated KOH and conductivity detection after suppression. Column Dionex lonPac AS11 diameter = 4 mm flow = 2.0 mL/min. Eluent 0.5 mM KOH for 2.5 min, 0.5 to 5.0 mM KOH from 2.5 to 6 min 5.0 to 38.2 mM KOH from 6 to 18 min. Peaks (1) quinate, (2) F, (3) acetate, (4) propanoate, (5) formate,...

The shikimate pathway is common to both plants and microorganisms (Figure 3-3). Shikimate is synthesized from the substrates phosphoewo/pyruvate (3.9) and erythrose 4-phosphate (3.17). These two precursors are derived from glycolysis and the pentose phosphate pathway, respectively, and are condensed to 3-deoxy-D-ara6/ o-heptulosonate 7-phosphate (DAHP 3.18) by the enzyme DAHP synthase. The subsequent steps result in the formation of 3-dehydro-quinate (3.19) by the enzyme 3-dehydroquinate synthase, 3-dehydroshikimate... 

The substitution of the phenyl ring necessary for the biosynthesis of coniferyl alcohol (3.79) and sinapyl alcohol (3.81) begins with the hydroxylation of C3. This is a conversion that requires the formation of the ester of /5-coumaroyl-CoA with D-quinate (3.73) or shikimate (3.74) catalyzed by the enzyme hydroxycinnamoyl-CoA shikimate/quinate hydroxy-cinnamoyl transferase (HCT Hoffmann et al., 2003). The hydroxylation of this ester intermediate is catalyzed by the enzyme /i-coumarovl-Co A 3 -hydroxylase (C3 H Schoch et al., 2001 Franke et al., 2002a,b). The resulting shikimate or quinate ester (3.75 3.76) is subsequently hydrolyzed by the same HCT, resulting in caffeoyl-CoA (3.36). 

Figure 3-9. Biosynthesis of monolignols. The enzymes involved in this pathway are ( ) hydroxycinnamoyl-CoA shikimate/quinate hydroxy-cinnamoyl transferase, (b) p-coumaroyl-CoA 3 -hydroxylase (E.C. 1.14.14.1), (c) caffeoyl-CoA O-methy 1 Iranslerasc (E.C. 2.1.1.104), (d) cinnamoyl-CoA reductase (E.C. 1.2.1.44) (e) cinnamyl alcohol dehydrogenase (E.C. 1.1.1.195), (f) coniferyl aldehyde/coniferyl alcohol 5-hydroxylase (E.C. 1.14.13), (g) coniferaldehyde/coniferyl alcohol O-methyltransferase (E.C. 2.1.1.68).

Hoffmann, L., Besseau, S., Geoffroy, P., Ritzenthaler, Ch., Meyer, D., Lapierre, C., Pollet, B., and Legrand, M., 2004, Silencing of hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxyltransferase affects phenylpropanoid biosynthesis, Plant Cell 16 1446-1465. 

Kuhnl, T., Koch, U., Heller, W., and Wellmann, E., 1987, Chlorogenic acid biosynthesis characterization of a light induced microsomal 5-0-(4-coumaroyl)-D-quinate/shikimate 3 -hydroxylase from carrot (Daucus carota L.) cell suspension cultures, Arch. Biochem. Biophys. 258 226-232. 

Figure 6-1. Oxidation of chlorogenic acid (6.4) by polyphenoloxidase (PPO), resulting in chlorogenoquinone (6.5), which can react with nucleophilic groups in proteins (6.6) to give the cross-linked compound 6.7, which can react with another protein molecule to yield 6.8. The quinate residue in structures 6.5, 6.7 and 6.8 is represented by R, whereas Ri and R2 indicate different amino acid residues.

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