1.1.1.282: quinate/shikimate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about quinate/shikimate dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.282
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1.1.1.282
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3-dehydroquinate
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lignin
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corynebacterium
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nad+-dependent
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glutamicum
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cosubstrate
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drug development
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dehydrogenases
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agriculture
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synthesis
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medicine
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pharmacology
- 1.1.1.282
- 3-dehydroquinate
- lignin
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corynebacterium
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nad+-dependent
- glutamicum
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cosubstrate
- drug development
- dehydrogenases
- agriculture
- synthesis
- medicine
- pharmacology
Reaction
Synonyms
cgl0424, cgR_0495, dehydroquinate dehydratase-shikimate dehydrogenase, More, NAD+ cofactor-specific QDH, NAD+-dependent enzyme quinate/shikimate dehydrogenase, NADP+ cofactor-specific QDH, NADP+-specific DHQD-QDH, PintaQDH, Poptr2, Poptr3, Poptr4, QDH, QSDH, qsuD, quinate dehydrogenase, quinate/shikimate 5-dehydrogenase, quinate/shikimate dehydrogenase, rifI, RifI2, SDH, SDH/QDH, sdhL, shikimate/quinate dehydrogenase, YdiB
ECTree
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General Information
General Information on EC 1.1.1.282 - quinate/shikimate dehydrogenase [NAD(P)+]
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evolution
malfunction
metabolism
physiological function
additional information
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members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. Plant SDHs are generally more similar to bacterial SDH/QDH YdiB (25-30% similarity) than to bacterial SDH AroE (21-28%)
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
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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
evolution
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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
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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
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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 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
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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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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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disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism
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
malfunction
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disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism
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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
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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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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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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QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization
physiological function
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quinate and its derivatives are protective secondary metabolites, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase
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 reduced efficiency of Corynebacterium glutamicum enzyme with shikimate as a substrate may also result in part from the flexibility of the catalytic group, Lys73, which adopts multiple conformations in the shikimate-liganded enzyme structure
physiological function
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Escherichia coli strain PB12.SA22 and the derivatives ydiB- and ydiB+ are evaluated for their ability to produce shikimate (SA), quinate (QA), 3-dehydroshikimate (DHS), and 3-dehydroquinate (DHQ) in batch culture fermentations growing in 1-l fermentors using 500 ml of a mineral broth supplemented with 25 g/l glucose and 15 g/l YE. Biomass and glucose consumption and the production of aromatic intermediates of the SA pathway, SA, QA, DHQ, and DHS are determined for all derivatives, overview. The highest production of DHQ and DHS is 0.07 and 0.074 g/l, respectively. SA and QA are produced during the early exponential stage, as these compounds are detected during the first 5 h of cultivation (SA = 0.49 g/l and QA = 0.38 g/l, respectively). In the stationary stage and until 20 h of cultivation, this strain consumes the remaining residual glucose. From this time until the end of fermentation, the supernatant concentration of detected SA shows no significant changes, reaching 8.2 g/l by the end of fermentation (50 h), whereas the final QA concentration is 1.52 g/l
physiological function
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inactivation of ydiB results in a 75% decrease in the molar yield of quinic acid and a 6.17% reduction in the yield of quinic acid (mol/mol) relative to shikimic acid with respect to the parental strain. The overexpression of ydiB causes a 500% increase in the molar yield of quinic acid and results in a 152% increase in quinic acid (mol/mol) relative to shikimic acid, with a sharp decrease in shikimic acid production
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. The reduced efficiency of Corynebacterium glutamicum enzyme with shikimate as a substrate may also result in part from the flexibility of the catalytic group, Lys73, which adopts multiple conformations in the shikimate-liganded enzyme structure
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physiological function
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Escherichia coli strain PB12.SA22 and the derivatives ydiB- and ydiB+ are evaluated for their ability to produce shikimate (SA), quinate (QA), 3-dehydroshikimate (DHS), and 3-dehydroquinate (DHQ) in batch culture fermentations growing in 1-l fermentors using 500 ml of a mineral broth supplemented with 25 g/l glucose and 15 g/l YE. Biomass and glucose consumption and the production of aromatic intermediates of the SA pathway, SA, QA, DHQ, and DHS are determined for all derivatives, overview. The highest production of DHQ and DHS is 0.07 and 0.074 g/l, respectively. SA and QA are produced during the early exponential stage, as these compounds are detected during the first 5 h of cultivation (SA = 0.49 g/l and QA = 0.38 g/l, respectively). In the stationary stage and until 20 h of cultivation, this strain consumes the remaining residual glucose. From this time until the end of fermentation, the supernatant concentration of detected SA shows no significant changes, reaching 8.2 g/l by the end of fermentation (50 h), whereas the final QA concentration is 1.52 g/l
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physiological function
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inactivation of ydiB results in a 75% decrease in the molar yield of quinic acid and a 6.17% reduction in the yield of quinic acid (mol/mol) relative to shikimic acid with respect to the parental strain. The overexpression of ydiB causes a 500% increase in the molar yield of quinic acid and results in a 152% increase in quinic acid (mol/mol) relative to shikimic acid, with a sharp decrease in shikimic acid production
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physiological function
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QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization
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enzyme RifI2 lacks a conserved C-terminal alpha-helix
additional information
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enzyme RifI2 lacks a conserved C-terminal alpha-helix
additional information
substrate binding site structure, overview. Quinate binding causes a slight closure of the N- and C-terminal domain of CglQSDH. Shikimate binding causes a alternative side-chain conformation of Lys73
additional information
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substrate binding site structure, overview. Quinate binding causes a slight closure of the N- and C-terminal domain of CglQSDH. Shikimate binding causes a alternative side-chain conformation of Lys73
additional information
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the enzymes have Gly residues instead of Ser residues in the active sites. The Ser-to-Gly conversion ompared to SDHs may generate extra space in the inferred Poptr isozymes active sites that can accommodate the hydroxyl group at the C1 position of quinate
additional information
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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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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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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
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
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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substrate binding site structure, overview. Quinate binding causes a slight closure of the N- and C-terminal domain of CglQSDH. Shikimate binding causes a alternative side-chain conformation of Lys73
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additional information
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enzyme RifI2 lacks a conserved C-terminal alpha-helix
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