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evolution
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a three-dimensional structural model of TgSDH predicts a high level of conservation in the core structure of the enzyme
evolution
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members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH1 belongs to group I, and clusters with four characterized DQD/SDHs: AtSDH, Poptr1, JrSDH, and NtSDH1, group members share about 75% sequence identity
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH2 belongs to group II, and clusters with Poptr2 and Poptr3, two characterized DQD/SDHs, and NtSDH2, group members share about 71% sequence identity
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH3 belongs to group III, group members share about 85% sequence identity, four of them from different species (VvSDH3, CasSDH2, FvSDH1, and EgSDH3) accumulate gallic acid-based tannins
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH4 belongs to group IV, and clusters with with Poptr5, a DQD/SDH characterized in Populus trichocarpa, group members share about 77% sequence identity
evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
evolution
Escherichia coli constitutively expresses two shikimate dehydrogenase paralogues, AroE and the NAD+ -dependent enzyme quinate/shikimate dehydrogenase (YdiB), sharing 25% sequence identity. While AroE is NADP+-dependent, YdiB uses NADP+ or NAD+. Contrary to AroE, YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate
evolution
four CsDQD/SDH isozyme proteins are cloned from Camellia sinensis. Three CsDQD/SDH isozymes show 3-dehydroshikimate (3-DHS) reduction and shikimate (SA) oxidation functions with individual differences between the catalytic efficiency of 3-DHS reduction and SA oxidation. Isozyme CsDQD/SDHa has higher catalytic efficiency for 3-DHS reduction than for SA oxidation, isozyme CsDQD/SDHd shows the opposite tendency, and isozyme CsDQD/SDHc has almost equal catalytic efficiency for 3-DHS reduction and SA oxidation. In vitro, Gallic acid (GA) is mainly generated from 3-DHS through nonenzymatic conversion. Isozymes CsDQD/SDHc and CsDQD/ SDHd genes are involved in GA synthesis
evolution
plant QDHs arose directly from bifunctional dehydroquinate dehydratase-shikimate dehydrogenases (DHQD-SDHs) through different convergent evolutionary events, detailed phylogenetic analysis, overview. Eudicot and conifer QDHs arose early in vascular plant evolution whereas Brassicaceae QDHs emerged late, process of recurrent evolution of QDH. This family of proteins independently evolved NAD+ and NADP+ specificity in eudicots. The acquisition of QDH activity by these proteins is accompanied by the inactivation or functional evolution of the DHQD domain, as verified by enzyme activity assays and as reflected in the loss of key DHQD active site residues
evolution
plant SDH enzymes are fused to dehydroquinate dehydratases (DQDs, EC 4.2.1.10) to form bifunctional DQD/SDH enzymes. The DQD activity is observed for EcDQD/SDH1, 2, and 3, but not for EcDQD/SDH4a. Among the active enzymes, EcDQD/SDH1 exhibits the highest DQD activity, followed by EcDQD/SDH2 (about 50% of the EcDQD/SDH1 activity) and EcDQD/SDH3 (about 5% of the EcDQD/SDH1 activity). For shikimate formation from 3-DHS as well as shikimate oxidation to 3-DHS, measurable catalytic activities are detected for EcDQD/SDH1-3, but the activities of EcDQD/SDH2 and 3 are less than 20% of those of EcDQD/SDH1. Regarding the cofactor, EcDQD/SDH1-3 have a clear preference for NADPH/NADP+ over NADH/ NAD+. In contrast, EcDQD/SDH4a and b lack shikimate formation activity. For the reverse reaction, the conversion of shikimate to 3-DHS, EcDQD/SDH4a and b display low enzymatic activity with a preference for NAD+ as the cofactor. Both EcDQD/SDH2 and 3 exhibit relatively high gallate formation activity, in contrast to the low activity of EcDQD/SDH1. The preferred cofactor in this reaction is NADP+
evolution
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the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
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the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
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the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
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the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
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the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
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the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
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evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
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evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
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evolution
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members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282
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evolution
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Escherichia coli constitutively expresses two shikimate dehydrogenase paralogues, AroE and the NAD+ -dependent enzyme quinate/shikimate dehydrogenase (YdiB), sharing 25% sequence identity. While AroE is NADP+-dependent, YdiB uses NADP+ or NAD+. Contrary to AroE, YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate
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evolution
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SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
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malfunction
a contact with the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Arabidopsis thaliana DHQ-SDH causes a substantial reduction in turnover rate
malfunction
in the ydiB knockout mutant, QA production is 6.17% relative to SA (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce QA production below 10% (mol/mol) relative to SA in culture fermentations for SA production. The inactivation of ydiB in Escherichia coli strain PB12.SA22 and the reduction in QA production support the role of YdiB in the synthesis of this compound from DHQ. In the absence of YdiB, the DHS concentration detected in supernatant cultures is maintained relatively constant during the stationary phase
malfunction
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mutation of Lys69 to alanine significantly reduces the catalytic efficiency of Helicobacter pylori SDH. Mutation of Lys69 triggers the movement of shikimate away from the active site of SDH, thereby disrupting the catalytic activity
malfunction
the mutation of residues Ser338 and NRT to Gly and DI/LD in the SDH unit is the reason for the low activity of isozyme CsDQD/SDHb for 3-DHS reduction and SA oxidation
malfunction
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in the ydiB knockout mutant, QA production is 6.17% relative to SA (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce QA production below 10% (mol/mol) relative to SA in culture fermentations for SA production. The inactivation of ydiB in Escherichia coli strain PB12.SA22 and the reduction in QA production support the role of YdiB in the synthesis of this compound from DHQ. In the absence of YdiB, the DHS concentration detected in supernatant cultures is maintained relatively constant during the stationary phase
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metabolism
aroE-encoded shikimate dehydrogenase catalyzes the forth reaction in the shikimate pathway
metabolism
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SKDH is one of the crucial enzymes in the biosynthesis of anthocyanin metabolites, overview
metabolism
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway, (B) the quinate pathway, (C) the aminoshikimate pathway, overview
metabolism
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in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway. (B) the quinate pathway. (C) the aminoshikimate pathway, overview
metabolism
in plants, the shikimate pathway provides aromatic amino acids that are used to generate numerous secondary metabolites, including phenolic compounds. In this pathway, shikimate dehydrogenases catalyse the reversible dehydrogenation of 3-dehydroshikimate to shikimate
metabolism
in plants, the shikimate pathway provides aromatic amino acids that are used to generate numerous secondary metabolites, including phenolic compounds. In this pathway, shikimate dehydrogenases catalyse the reversible dehydrogenation of 3-dehydroshikimate to shikimate. Gallic acid metabolism in grape berry tissues along development, overview
metabolism
the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
metabolism
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the enzyme is part of the AROM complex, a large pentafunctional polypeptide, which catalyzes steps two through six of the shikimate pathway in fungi. This complex has the following functional domains (from N- to C-terminus): dehydroquinate synthase, 5-enolypyruvylshikimate-3-phosphate synthase, shikimate kinase, dehydroquinate dehydratase, and SDH. These domains catalyze steps 2, 6, 5, 3, and 4 of the pathway, respectively. The first and last enzymes of the fungal shikimate pathway,3-deoxy-D-arabinoheptulosonate 7-phosphate synthase and chorismate synthase, are discrete enzymes
metabolism
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the shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. 3-Dehydroquinate is the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. Reactions comprising the shikimate/quinate cycle, overview
metabolism
3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) is a key enzyme for catalyzing the conversion of 3-dehydroshikimate (3-DHS) to shikimate (SA). It also potentially participates in gallic acid (GA) synthesis in a branch of the SA pathway. Gallic acid (GA) is a precursor for polyphenol synthesis. The CsDQD/SDHc and CsDQD/ SDHd genes are involved in GA synthesis. In plants, DQD/SDH, a bifunctional enzyme, is crucial in the third and fourth reversible reactions in the SA pathway. Biosynthetic pathway of gallic acid and shikimic acid in plants, overview. GA could be spontaneously generated from 3-DHS in the enzymatic or nonenzymatic CsDQD/SDHs assay when using 3-DHS and the coenzyme NADP+ as substrates
metabolism
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link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
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link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
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link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
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link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
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link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
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link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
shikimate dehydrogenase (HpSDH) is a key enzyme in the shikimate pathway of Helicobacter pylori, which catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate
metabolism
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shikimate dehydrogenase is one of the enzymes involved in the initial steps of the biosynthesis of amino acids such as histidine, tryptophan, tyrosine, phenylalanine, lysine, and aspartic acid
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism. Isozymes EcDQD/SDH2 and 3 from Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. In Eucalyptus camaldulensis, EcDQD/SDH2 and 3 are co-expressed with UGT84A25a/b and UGT84A26a/b involved in hydrolyzable tannin biosynthesis, catalyze the synthesis of beta-glucogallin
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism. Isozymes EcDQD/SDH2 and 3 from Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. In Eucalyptus camaldulensis, EcDQD/SDH2 and 3 are co-expressed with UGT84A25a/b and UGT84A26a/b involved in hydrolyzable tannin biosynthesis, they catalyze the synthesis of beta-glucogallin
metabolism
the enzyme is active in the shikimic acid pathway, which is present in bacteria, fungi, plants and in certain apicomplexan parasites but is absent from humans, pathway overview
metabolism
the outer peels of Punica granatum fruits possess two groups of polyphenols: anthocyanins (ATs) and hydrolysable tannins (HTs). Their biosynthesis intersects at 3-dehydroshikimate (3-DHS) in the shikimate pathway by the activity of shikimate dehydrogenase (SDH), which converts 3-DHS to shikimate (providing the precursor for AT biosynthesis) or to gallic acid (the precursor for HTs biosynthesis) using NADPH or NADP+ as a cofactor. The outer fruit peel is subjected to light/dark treatment and osmotic stresses (imposed by different sucrose concentrations) showing that light with high sucrose promotes the synthesis of ATs, while dark at the same sucrose concentration promotes the synthesis of HTs. Role of PgSDH in the branch point leading to gallic acid and shikimate, detailed overview. The activity of isozymes PgSDH3, PgSDH3a and PgSDH4 may lead to the synthesis of phenols required for protecting the cells from osmotic stress. Since PgSDH3.2 has a plastid transit peptide, it may mainly use the NADP+ that accumulates in the dark in plastids, while PgSDH3.1, PgSDH3a and PgSDH4 use this cofactor that mainly accumulates during stress
metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
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metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
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metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
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metabolism
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the shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. 3-Dehydroquinate is the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. Reactions comprising the shikimate/quinate cycle, overview
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metabolism
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the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
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physiological function
a strain deficient in isoform qsuD does not grow on either shikimate or quinate as sole carbon sources but grows largely unhindered on glucose
physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes, the enzyme reaction represents the fourth step of the shikimate pathway
physiological function
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the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and E.C. 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
physiological function
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the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and EC 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
physiological function
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Toxoplasma gondii encodes a large pentafunctional polypeptide known as the AROM complex which catalyzes five reactions in the shikimate pathway, a metabolic pathway required for the biosynthesis of the aromatic amino acids and a promising target for anti-parasitic agents. The shikimate dehydrogenase domain (TgSDH) from the Toxoplasma gondii AROM complex catalyzes the NADP+-dependent oxidation of shikimate in the absence of the remaining AROM domains
physiological function
3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) is a key enzyme for catalyzing the conversion of 3-dehydroshikimate (3-DHS) to shikimate (SA). It also potentially participates in gallic acid (GA) synthesis in a branch of the SA pathway. Quantitative RT-PCR analysis shows that CsDQD/SDHc and CsDQD/SDHd expression is correlated with GA and 1-O-galloyl-beta-D-glucose accumulation in Camellia sinensis. The SA pathway is important to plant growth, development, and defense. Polyphenols in tea plants, including phenolic acids, catechins, and flavonol derivatives, not only determine the mouthfeel of tea infusions but also provide health benefits
physiological function
role of shikimate dehydrogenase in controlling the production of anthocyanins (ATs) and hydrolysable tannins (HTs) in the outer peels of pomegranate, Punica granatum. The biosynthesis of HTs and ATs competes for the same substrate, 3-DHS, and that SDH activity is regulated not only by the NADPH/NADP+ ratio, but also by the expression of the PgSDHs
physiological function
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shikimate dehydrogenase (SDH) catalyzes the reversible, NADPH-dependent reduction of 3-dehydroshikimate to shikimate, involved in the shikimate pathway
physiological function
shikimate dehydrogenase (SDH) from Mycobacterium tuberculosis (MtbSDH), encoded by the aroE gene, is essential for viability of Mycobacterium tuberculosis
physiological function
the tree species Eucalyptus camaldulensis shows exceptionally high tolerance against aluminum, a widespread toxic metal in acidic soils. In the roots of Eucalyptus camaldulensis, aluminum is detoxified via the complexation with oenothein B, a hydrolyzable tannin. The biosynthesis of oenothein B involves dehydroquinate dehydratase/shikimate dehydrogenases (EcDQD/SDHs) which catalyzes the formation of gallate, the phenolic constituent of hydrolyzable tannins
physiological function
the tree species Eucalyptus camaldulensis shows exceptionally high tolerance against aluminum, a widespread toxic metal in acidic soils. In the roots of Eucalyptus camaldulensis, aluminum is detoxified via the complexation with oenothein B, a hydrolyzable tannin. The biosynthesis of oenothein B involves dehydroquinate dehydratase/shikimate dehydrogenases (EcDQD/SDHs) which catalyzes the formation of gallate, the phenolic constituent of hydrolyzable tannins. Two enzymes, EcDQD/SDH2 and 3, in Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. EcDQD/SDH2 and 3 maintain DQD and SDH activities, resulting in a 3-dehydroshikimate supply for gallate formation
physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
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physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
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physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
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physiological function
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the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and E.C. 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
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physiological function
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the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and EC 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
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physiological function
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shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
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physiological function
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a strain deficient in isoform qsuD does not grow on either shikimate or quinate as sole carbon sources but grows largely unhindered on glucose
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additional information
the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans
additional information
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the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans
additional information
in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ-SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ-SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processe. Crystallization of the Arabidopsis thaliana protein with shikimate bound in the SDH domain and tartrate (a component of the crystallization solution) in the DHQ domain reveals a V-shaped orientation of the domains. Addition of NADP+ to DHQSDH crystals already containing shikimate in the SDH domain results in the production of 3-dehydroshikimate by the SDH domain and the transfer of the compound to the DHQ active sites
additional information
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in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQSDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQSDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processes
additional information
modelling of steady state and dynamic fluxes into pentose phosphate pathway and the flux split ratio into glycolysis and pentose phosphate pathway in Saccharomyces recombinantly expressing Escherichia coli shikimate dehydrogenase, overview
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
analysis of the catalytic active site in the crystal structure of HpSDH in complex with its substrate NADPH and product shikimate. The site can be divided into three spatially separated subpockets that separately correspond to the binding regions of shikimate, NADPH dihydronicotinamide moiety, and NADPH adenine moiety
additional information
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analysis of the catalytic active site in the crystal structure of HpSDH in complex with its substrate NADPH and product shikimate. The site can be divided into three spatially separated subpockets that separately correspond to the binding regions of shikimate, NADPH dihydronicotinamide moiety, and NADPH adenine moiety
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
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EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
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EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
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EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
molecular docking calculations and molecular dynamics (MD) simulations for enzyme-substrate interaction and binding structure analysis, model of DHS/NADPH/MtbSDH ternary complex, wild-type and mutant enzymes, detailed overview. Lys69 plays a dual role, in positioning NADPH and in catalysis. Asp105 plays a crucial role in positioning both the epsilon-amino group of Lys69 and nicotinamide ring of NADPH for MtbSDH catalysis but makes no direct contribution to DHS binding. Ala213 is the selection key for NADPH binding with the nicotinamide ring in the proS, rather than proR, conformation in the MtbSDH complex. Residues Ser18, Thr65, Lys69, Gln243, and Gln247 forming hydrogen bonds to 3-dehydroshikimate (DHS)
additional information
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molecular docking calculations and molecular dynamics (MD) simulations for enzyme-substrate interaction and binding structure analysis, model of DHS/NADPH/MtbSDH ternary complex, wild-type and mutant enzymes, detailed overview. Lys69 plays a dual role, in positioning NADPH and in catalysis. Asp105 plays a crucial role in positioning both the epsilon-amino group of Lys69 and nicotinamide ring of NADPH for MtbSDH catalysis but makes no direct contribution to DHS binding. Ala213 is the selection key for NADPH binding with the nicotinamide ring in the proS, rather than proR, conformation in the MtbSDH complex. Residues Ser18, Thr65, Lys69, Gln243, and Gln247 forming hydrogen bonds to 3-dehydroshikimate (DHS)
additional information
only four amino acid residues likely to contribute to specificity for one substrate instead of the other, namely S336, S338, T381 and Y550, all of which would be in the direct vicinity of the quinate C1-hydroxyl. Amino acid S336 has previously been shown by mutational analysis to be critical for shikimate binding. The size of the amino acid side chain at position 381 is a key determinant of substrate specificity
additional information
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the conserved Lys69 plays an important role in the catalytic activity of Helicobacter pylori SDH, structure-function analysis using the structure of SDH in complex with shikimate and NADP+ (PDB ID 3PHI). Two-layered ONIOM-based quantum mechanics/molecular mechanics (QM/MM) calculation and molecular dynamics (MD) simulations are performed to explore the role of Lys69 in SDH activity, overview. In addition to act as a catalytic base, the conserved Lys69 plays an additional, important role in the maintenance of the substrate shikimate in the active site, facilitating the catalytic reaction between the cofactor NADP+ and shikimate. Shikimate forms hydrogen bonds with Ser16, Ser18, and Tyr210. The C3-hydroxyl group of shikimate is hydrogen bonded to the side chain amide group of Gln237. The C4-hydroxyl group of shikimate donates hydrogen bonds with both the side chain amide group of Asn90 and the carboxylate group of Asp105. The C5-hydroxyl group of shikimate makes hydrogen bonds with the side chain hydroxyl group of Thr65 and the side chain ammonium group of Lys69. Comparison of active site structures of wild-type and mutant K69A enzymes
additional information
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three-dimensional stucture homology modelling (PMDB ID PM0080741), model refinement and validation, overview
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
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