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Information on EC 1.1.1.B61 - shikimate dehydrogenase [NADP]+
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.B61
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
shikimate dehydrogenase [NADP]+
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-dehydroshikimate + NADPH + H+ = shikimate + NADP+
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SYSTEMATIC NAME
IUBMB Comments
shikimate:NADP+ 3-oxidoreductase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
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trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
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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
metabolism
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
additional information
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
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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
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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
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 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 DHQ–SDH 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 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 processes
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
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additional information
?
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The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
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additional information
?
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the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
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additional information
?
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The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
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additional information
?
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The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate. Under saturating conditions, Poptr5 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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for Poptr5, no activity with shikimate is detectable in the presence of NAD+ even with elevated enzyme concentrations
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Epicatechin gallate
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inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epigallocatechin gallate
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inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
additional information
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screening for polyphenolc enzyme inhibitors, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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Michaelis-Menten kinetics
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0.321
shikimate
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with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
Epicatechin gallate
Arabidopsis thaliana
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pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
0.0021
epigallocatechin gallate
Arabidopsis thaliana
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pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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poplar DQD/SDHs have distinct expression profiles, organ-specific expression of poplar DQD/SDHs, overview
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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the SDH domain is connected via its N-terminus to the DHQ module
additional information
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the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. 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
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the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. 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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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged DQD/SDH isozyme 5 from Escherichia coli strain M15 by nickel affinity chromatography
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recombinant His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus by nickel affinity chromatography and dialysis
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus
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recombinant His6-tagged DQD/SDH isozyme 5 overexpression in Escherichia coli strain M15
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.B61)
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