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Results 1 - 10 of 21 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24evolution quercetinases are metal-dependent dioxygenases of the cupin superfamily 742192
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24evolution the ring-cleaving dioxygenase belongs to the cupin superfamily, characterized by a six-stranded beta-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. The cupin domain comprises two conserved amino acid motifs with the consensus sequences G(X)5HXH(X)3-4E(X)6G (motif 1) and G(X)5-7PXG(X)2H(X)3N -, 724015
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24malfunction replacement of individual amino acids of the 3His/1Glu metal binding motif by alanine drastically reduces or abolishes quercetinase activity and affects its structural integrity. Only substitution of the glutamate ligand (E76) by histidine results in Ni- and Co-QueD variants that retain the native fold and show residual catalytic activity 742192
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24malfunction the mutational removal of Glu73 causes a loss of enzyme activity 742437
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24malfunction the pathogenicity of VdQase knock-out mutants generated through Agrobacterium tumefasciens-mediated transformation is significantly reduced on susceptible potato cultivar Kennebec compared to wild-type isolates. Phenotype with a higher accumulation of flavonols in the stems of infected potatoes and a higher concentration of rutin in the leaves in response to the VdQase mutants as compared to wild-type isolates -, 742592
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24metabolism compounds TpMesMFla (TpMes = hydrotris(3-mesityl)pyrazolylborate, M = Mn, Fe, Co, Ni, Zn, Fla = 3-hydroxyflavonolate) as models for 2,4-quercetin dioxygenase. The structures differ in the degree of delocalization in the chelate ring formed through the binding of the two O donors of the flavonolate to the metal center, the resulting trend (Zn/Fe > Co > Mn > Ni) is, not in line with the one that found when investigating the redox properties of the complexes by cyclic voltammetry (Zn > Fe > Ni > Co > Mn). The complexes exhibit exceptionally well-behaved quasi-reversible redox transitions. After the O2 reaction, salicylic acid is one of the products 764837
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24metabolism design of model ligands 2NCOO, 3 N, 3NCOO, 4 N (L2NCOOH: 2-((benzyl(pyridin-2-ylmethyl)amino)methyl)benzoic acid, L3N: N-benzyl-1-(pyridin-2-yl)-N-(pyridin-2-ylmethyl)methanamine, L3NCOOH: 2-{[bis(pyridin-2-ylmethyl)amino]methyl}benzoic acid, L4N: tris(pyridin-2-ylmethyl)amine) and their complexes [CoIILn(fla)] (n: 2NCOO (1), 3 N (2), 3NCOO (3), 4 N (4); fla: 3-flavonolate) as ES models of the Co(II)-containing quercetin 2,4-dioxygenase. [CoLn(fla)] exhibits higher single turnover O2 reactivity to produce products similar to the enzymatic reaction, and the decreasing order of reactivity is 3 > 4 > 1 > 2. The reaction rate constant k shows linear correlation with E1/2(CoIII/II) and Epa(fla-/fla radical) 764501
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24metabolism during oxidative ring-cleaving, electron transfer occurs from the quercetin to dioxygen via the nickel ion. Both the dioxygen and substrate are activated by binding to the nickel ion. The catalytic reaction includes the first attack of the Od atom on the quercetin to form the C-O bond, the movement of the coordinated Op atom, the formation of a five-membered heterocyclic ring, and the synergetic cleavage of the O-O bond and C-C bonds. The movement of the coordinated Op atom is the rate-limiting step 764415
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24metabolism the nickel(II) flavonolate complex bearing a tridentate macrocyclic ligand, [NiII(Me3-TACN)(Fl)(NO3)](H2O) (Me3-TACN = 1,4,7-trimethyl-1,4,7-triazacyclononane, Fl = 3-hydroxyflavone) is a functional model for QueD. The complex shows two isomers with respect to the direction of a flavonolate ligand. Two isomers commonly are in the octahedral geometry with a bidentate of flavonolate and a monodentate of nitrate as well as a tridentate binding of the Me3-TACN ligand. The spin state is a triplet state, and the two singly occupied molecular orbitals (SOMOs) lie energetically lower than the highest (doubly) occupied molecular orbital (HOMO). The HOMO shows an electron density localized in the flavonolate ligand 765205
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.24metabolism the reaction takes place via three major steps: attack of the superoxide on the C2 of the substrate pyrone ring to generate a Ni(II)-peroxide intermediate, formation of the second C-O bond between C4 and the peroxide to produce a peroxide bridge, and simultaneous cleavage of the C2-C3, C3-C4, and O1-O2 bonds with the formation of 2-protocatechuoylphloroglucinol carboxylic acid and carbon monoxide. The third step is rate-limiting, with a barrier of 17.4 kcal/mol. For the second C-O bond formation, an alternative pathway is that the peroxide attacks the C3 of the substrate pyrone ring, leading to the formation of a four-membered ring intermediate, which then undergoes concerted C2-C3 and O1-O2 bond cleavages to produce an alpha-keto acid. This pathway is associated with a barrier of 30.6 kcal/mol. When Glu74 is protonated, the 2,3-dioxygenolytic pathway, however, has a lower barrier (21.8 kcal/mol) than the 2,4-dioxygenolytic pathway 765534
Results 1 - 10 of 21 > >>