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Enzyme Nomenclature
Information on EC 1.1.1.25 - shikimate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.25
Word Map on EC 1.1.1.25
- 1.1.1.25
- 3-dehydroshikimate
- drug development
-
allozyme
- dahp
-
pentafunctional
-
5-enolpyruvylshikimate
- 3-dehydroquinase
- diagnostics
- agriculture
- analysis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.25
-
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RECOMMENDED NAME
GeneOntology No.
shikimate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
-
-
-
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
active site structure, reaction and kinetic mechanisms
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
conserved residues Asp103 and Lys67 are important for catalysis in all three paralogues, kinetic mechanism of paralogue HI0607 and substrate binding site
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
active-site base is K92. After the binding of quinate and NAD+, the oxygen of the C3-OH of quinate forms a hydrogen bond to the side chain of the conserved T88 and K92 functions as the active-site base to remove the proton on the C3-OH. Simultaneously,a hydride is transferred from C3 of quinate to NAD+
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
steady-state ordered bi-bi kinetic mechanism. The hydride transferred from NADPH and protons transferred from the solvent in the catalytic cycle are not significantly rate limiting in the overall reaction. Both hydride and proton transfers are concerted, and acid/base chemistry takes place in catalysis and substrate binding
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the active enzyme for dehydrogenation of shikimate contains a deprotonated K70 residue, a deprotonated D106, and a protonated Y216. The hydride transfer and the deprotonation of the 3-hydroxyl group of shikimate proceed in a concerted manner. K70 functions as a general base and becomes protonated in the dehydrogenation reaction. The proton is then transferred to the bulk solvent via the short proton-conducting wire. D106 plays a critical role in the transfer of the proton to the bulk solvent
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the pro-R hydrogen of the nicotinamide C4 is 3.35 A from the C3 of shikimate. The catalytic K385 and D423 residues are proximal to the C3-hydroxyl of shikimate, which is deprotonated in the oxidation reaction. The enzyme adopts a concave architecture that places the active sites in a face-to-face arrangement
-
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding, overview
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the enzyme catalysis follows a sequential random mechanism, enzyme catalysis depends on acid-basic amino acids
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shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
the enzyme catalysis follows a sequential random mechanism, enzyme catalysis depends on acid-basic amino acids
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
shikimate:NADP+ 3-oxidoreductase
NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4].
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CAS REGISTRY NUMBER
COMMENTARY
9026-87-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
Uniprot
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
Uniprot
trees in Dabrowa Forest District, Pniewy Forest Division, regional directorate of state forests in Poznan, Poland
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-
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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three paralogues: YdiB, AroE, and the shikimate dehydrogenase-like HI0607
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-
wild-tpe and clinical Mtb strains MDRTB and RDRTB exhibiting resistant profiles to isoniazid and rifampin
UniProt
wild-tpe and clinical Mtb strains MDRTB and RDRTB exhibiting resistant profiles to isoniazid and rifampin
UniProt
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
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
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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; 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; 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; 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
-
a three-dimensional structural model of TgSDH predicts a high level of conservation in the core structure of the enzyme
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
-
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
-
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
-
metabolism
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SKDH is one of the crucial enzymes in the biosynthesis of anthocyanin metabolites, overview
metabolism
aroE-encoded shikimate dehydrogenase catalyzes the forth reaction in 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
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
-
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
metabolism
the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
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
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; 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; 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; 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
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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 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
-
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
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
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, the enzyme reaction represents the fourth step of the shikimate pathway
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
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
-
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
-
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
-
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
-
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
-
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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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
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
-
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
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
-
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
3-dehydroshikimate + NADH
shikimate + NAD+
-
SDH reaction, very low activity with NAD+
-
-
r
quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
-
DQD reaction
-
-
r
3-dehydroquinate + NADH + H+
quinate + NAD+
-
-
-
r
3-dehydroquinate + NADPH + H+
quinate + NADP+
-
-
-
r
3-dehydroquinate + NADPH + H+
quinate + NADP+
-
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NADH + H+
shikimate + NAD+
less than 1% of the rate with 3-dehydroquinate
-
-
r
3-dehydroshikimate + NADH + H+
shikimate + NAD+
less than 1% of the rate with 3-dehydroquinate
-
-
r
3-dehydroshikimate + NADPH
?
-
pathway of biosynthesis of aromatic amino acids
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
NADH may substitute for NADPH
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
structure of the enzyme is a compact alpha/beta sandwich with two distinct domains, responsible for binding substrate and NADP cofactor, respectively
-
-
?
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
in contrast to shikimate, quinate may form a hydrogen bond to the NAD+, and the hydroxyl group of a active-site threonine hydrogen bonds to quinate more effectively than shikimate resulting in a lower Michaelis constant and higher catalytic efficiency for quinate
-
-
?
quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
the fourth enzyme in the shikimate pathway
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
reversible activity of YdiB, no activity with paralogue HI0607
-
-
r
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
-
-
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH
-
assay at 24°C, pH 9.0
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
analysis of the 3-dehydroshikimate binding site
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
additional information
?
-
-
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
-
-
-
additional information
?
-
-
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities
-
-
-
additional information
?
-
-
no activity with quinate
-
-
-
additional information
?
-
usage of recombinant shikimate dehydrogenase as sensor reaction for determination of the cytosolic NADPH/NADP ratio in Saccharomyces cerevisiae, quantitative measurements of physiological variables in the cytosolic compartment by GC-MS/MS, cytosolic NADPH/NADP ratio in batch experiments, method, overview
-
-
-
additional information
?
-
-
fourth enzyme in the shikimate biosynthetic pathway
-
-
-
additional information
?
-
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
-
additional information
?
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
-
additional information
?
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
-
additional information
?
-
-
the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
-
-
-
additional information
?
-
the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
-
-
-
additional information
?
-
the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
-
-
-
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/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
-
-
-
additional information
?
-
-
under saturating conditions, Poptr1 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
-
-
-
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/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
-
-
-
additional information
?
-
-
under saturating conditions, Poptr1 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
-
-
-
additional information
?
-
broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
-
-
-
additional information
?
-
broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
-
-
-
additional information
?
-
no activity with quinate
-
-
-
additional information
?
-
even in the presence of a high concentration of quinate (4 mM), SDH displays no activity using either NADP+ or NAD+ as a cofactor
-
-
-
additional information
?
-
the SDH domain from the Toxoplasma gondii is part of the AROM complex. No activity with quinate
-
-
-
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
-
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
-
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
-
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
-
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
-
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
-
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
-
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
-
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
-
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
-
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
-
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
-
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
-
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
-
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
-
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
quinate + NAD+
3-dehydroquinate + NADH + H+
Q88GF6, Q88IJ7, Q88JP1, Q88K85, Q88RQ5
the fourth enzyme in the shikimate pathway
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
reversible activity of YdiB, no activity with paralogue HI0607
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Q56S04
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
Q56S04
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NADPH
?
-
pathway of biosynthesis of aromatic amino acids
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Q88GF6, Q88IJ7, Q88JP1, Q88K85, Q88RQ5
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
P07547
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Q58484
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A1K3RIC7
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A1K3RIC7
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A1K3RIC7
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Q88GF6, Q88IJ7, Q88JP1, Q88K85, Q88RQ5
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Q88IJ7
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Q5HNV1
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A168S2B8, A0A168S2G5, A0A168S2H6, D7TUX1
-
-
-
r
additional information
?
-
-
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
-
-
-
additional information
?
-
-
fourth enzyme in the shikimate biosynthetic pathway
-
-
-
additional information
?
-
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
-
additional information
?
-
Q6PUF9
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
-
additional information
?
-
Q6PUG0
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
-
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/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
-
-
-
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
turnover number decreases by more than 300fold when NADP+ is used instead of NAD+, regardless of substrate shikimate or quinate
NADP+
-
high affinity for the enzyme, the residues Gly130 and Ala131 are present in the N-terminal of the helix and those make positive electrostatic interactions with the phosphates of NADP cofactor
NADP+
-
specificity of TgSDH for NADP+ is consistent with the presence of the NRTXXR motif identified in the primary sequence of the protein
NADPH
binding site determinatiion and binding mode analysis, AroE contains a Rossmann fold NADPH binding domain
additional information
-
dinucleotide cofactor binding domain structure is a Rossmann fold
-
additional information
NADH shows about 2% of the activity with NADPH; NADPH shows about 2.5% of the activity with NADPH
-
additional information
-
NADH shows about 2% of the activity with NADPH; NADPH shows about 2.5% of the activity with NADPH
-
additional information
cofactor binding might trigger domain movement
-
additional information
-
the highest enzyme activity is observed with NADP+, and activity drops by 96% when replacing NADP+ with NAD+ for Poptr1
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
paralogue HI0607 is not affected by 5 mM of Zn2+, Ca2+, Mg2+, or Mn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2,4-triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.023 mg/ml
2,2'-bithiophene-5-carboxylic acid
-
the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
-
2,2-bisepigallocatechin gallate
about 50% inhibition at 0.0025 mM
-
2-([2-([2-([2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl)-1,3-benzothiazol-6-yl]amino)2-oxoethyl]sulfanyl)-N-(2-naphthyl)acetamide
IC50: 0.0029 mM, competitive inhibition with respect to shikimate, noncompetitive to NADP+, potent antibacterial activity
3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate
IC50: 0.0039 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+
3-(3-fluoropyridin-4-yl)-6-(phenoxymethyl)-1,2,4-triazolo[3,4-b]-1,3,4-thiadiazole
-
3-(4-bromophenyl)-6-((2,4-dichlorophenoxy)methyl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0396 mg/ml
3-(4-bromophenyl)-6-((2-methyl-4-chlorophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0216 mg/ml
3-(4-bromophenyl)-6-((4-chlorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0363 mg/ml
3-(4-bromophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0795 mg/ml
3-(4-bromophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0120 mg/ml
3-(4-bromophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0586 mg/ml
3-(4-chlorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.168 mg/ml
3-(4-chlorophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 5.052 mg/ml
3-(4-chlorophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.00937 mg/ml
3-(4-fluorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
3-(4-fluorophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0663 mg/ml
3-(beta-naphthylmethyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0407 mg/ml
6-((2,4-dichlorophenoxy)methyl)-3-(3-fluoropyridin-4-yl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
-
6-((4-bromophenoxy)methyl)-3-(4-bromophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0144 mg/ml
6-((4-bromophenoxy)methyl)-3-(4-chlorophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.00682 mg/ml
6-((4-fluorophenoxy)methyl)-3-(beta-naphthylmethyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0277 mg/ml
6-hydroxy-2,3-dihydrobenzo[b]furan-3-one
-
the inhibitor is identified by virtual screeening, 99% inhibition at 0.2 mM, mixed-type inhibition versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
-
7-hydroxy-2,2,8-trimethyl-2,3-dihydro-4H-chromen-4-one
-
the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
-
aurintricarboxylic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
butyl 2-([3-(2-naphthyloxy)4-oxo-2-(trifluoromethyl)4H-chromen-7-yl]oxy)propanoate
IC50: 0.0134 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+, potent antibacterial activity
cardiolipin
lower inhibitry potency, about 25% inhibition at 0.0025 mM
diethylenetriamine pentaacetic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
hydroquinone
lower inhibitry potency, about 25% inhibition at 0.0025 mM
maesaquinone diacetate
IC50: 0.0035 mM, noncompetitive inhibition with respect to shikimate and NADP+
merbromin
lower inhibitry potency, about 25% inhibition at 0.0025 mM
NADP+
product inhibition, competitive versus NADPH, noncompetitive versus 3-dehydroshikimate
nordihydroguaiaretic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
pyridoxine
lower inhibitry potency, about 25% inhibition at 0.0025 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
31% inhibition at 0.2 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
-
31% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
49% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
-
49% inhibition at 0.2 mM
3-ethyl-3,4-dihydro-2H-1-benzopyran
31% inhibition at 0.2 mM
4-[(morpholin-4-yl)methyl]benzoic acid
31% inhibition at 0.2 mM
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
29% inhibition at 0.2 mM
curcumin
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
33% inhibition at 0.2 mM
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
-
33% inhibition at 0.2 mM
p-chloromercuribenzoate
-
biphasic inhibition: first rapid inhibition leading to loss of 70% activity, then within 5 min loss of the remaining 30% activity, inhibition can be partially hindered by thiols and chloride
shikimate
shikimate synthesis decreases with increasing shikimate concentration. The relative activity halves at about 1.4 mM shikimate; shikimate synthesis decreases with increasing shikimate concentration. The relative activity halves at about 1.4 mM shikimate
shikimate
product inhibition, noncompetitive versus NADPH, competitive versus 3-dehydroshikimate
[2-[2-(dimethylamino)ethoxy]phenyl]methanol
45% inhibition at 0.2 mM
additional information
not inhibitory: quinate; not inhibitory: quinate
-
additional information
-
not inhibitory: quinate; not inhibitory: quinate
-
additional information
-
antibacterial activity of inhibitors, overview
-
additional information
antibacterial activity of inhibitors, overview
-
additional information
structure-activity relationship studies on 1,2,4-triazolo[3,4-b][1,3,4]thiadiazoles as inhibitors of shikimate dehydrogenase, 3,6-disubstituted triazolothiadiazoles synthesis, overview. The compounds exhibit cytotoxicity against Vero and Hep-G2 cellss, IC50 and MIC values
-
additional information
-
screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
-
additional information
screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzo-thiadiazole-7-carbothioic acid S-methyl ester
-
activates the enzymes of the anthocyanin metabolism, including the shikimate dehydrogenase, and increases the anthocyanin content in strawberries after harvest, with SKDH playing a crucial role
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.046
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.157
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
186
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH4
0.572
NAD+
pH 8.8, presence of 2 mM shikimate
1.083
NAD+
pH 8.8, presence of 2 mM quinate
5.4
NAD+
pH 8.8, presence of 2 mM shikimate
5.43
NAD+
pH 8.8, presence of 2 mM shikimate
0.0073
NADP+
pH 8.8, presence of 2 mM shikimate
0.023
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.038
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.0426
NADP+
-
pH not specified in the publication, 25°C, with shikimate
0.0538
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.112
NADP+
pH 8.8, presence of 2 mM shikimate
0.114
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.217
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.783
quinate
pH 8.8, presence of 2 mM NAD+
0.0046
shikimate
pH 8.8, presence of 2 mM NADP+
0.027
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.0375
shikimate
-
pH not specified in the publication, 25°C, with NADP+
0.07
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.0786
shikimate
pH 8.8, presence of 2 mM NAD+
0.105
shikimate
pH 8.8, presence of 2 mM NADP+
0.1468
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.155
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.223
shikimate
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.351
shikimate
pH 8.8, presence of 2 mM NAD+
0.422
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
4.2
shikimate
pH 8.8, presence of 2 mM NAD+
additional information
additional information
-
kinetic profile of the recombinant AroE, overview
-
additional information
additional information
steady-state kinetics of recombinant AroE
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NAD+; no measurable activity with NADH+; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NAD+; no measurable activity with NADH+; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NAD+; no measurable activity with NADH+; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NAD+; no measurable activity with NADH+; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NAD+; no measurable activity with NADH+; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate; no measurable activity with shikimate
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
the enzyme shows Michaelis-Menten kinetics toward both substrates shikimate and NADP+, kinetic analysis, sequential random mechanism, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.62
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
95.85
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
6.72
NAD+
pH 8.8, presence of 2 mM shikimate
40.7
NAD+
pH 8.8, presence of 2 mM quinate
61.1
NAD+
pH 8.8, presence of 2 mM shikimate
97.1
NAD+
pH 8.8, presence of 2 mM shikimate
5.3
NADP+
pH 8.8, presence of 2 mM shikimate
19.78
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
26.11
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
28.89
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
30.7
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
146.2
NADP+
-
pH not specified in the publication, 25°C, with shikimate
239
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
261.5
NADP+
pH 8.8, presence of 2 mM shikimate
37.7
quinate
pH 8.8, presence of 2 mM NAD+
1.99
shikimate
pH 8.8, presence of 2 mM NAD+
5.16
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
5.8
shikimate
pH 8.8, presence of 2 mM NADP+
7.56
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
11.72
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
26.12
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
31.2
shikimate
pH 8.8, presence of 2 mM NAD+
55.7
shikimate
pH 8.8, presence of 2 mM NAD+
94.55
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
135.8
shikimate
-
pH not specified in the publication, 25°C, with NADP+
266.2
shikimate
pH 8.8, presence of 2 mM NADP+
additional information
additional information
no measurable activity with NAD+; no measurable activity with NADH; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NADH; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NADH; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NADH; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate
-
additional information
additional information
no measurable activity with NAD+; no measurable activity with NADH; no measurable activity with NADH+; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with quinate; no measurable activity with shikimate
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
186
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
611
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
262
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
537
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
680
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
862
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
1113
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
18
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
76
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
178
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
189
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
1051
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic study of the enzyme-inhibitor complexes
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0029
2-([2-([2-([2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl)-1,3-benzothiazol-6-yl]amino)2-oxoethyl]sulfanyl)-N-(2-naphthyl)acetamide
Helicobacter pylori
Q56S04
IC50: 0.0029 mM, competitive inhibition with respect to shikimate, noncompetitive to NADP+, potent antibacterial activity
0.0039
3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate
Helicobacter pylori
Q56S04
IC50: 0.0039 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+
0.0134
butyl 2-([3-(2-naphthyloxy)4-oxo-2-(trifluoromethyl)4H-chromen-7-yl]oxy)propanoate
Helicobacter pylori
Q56S04
IC50: 0.0134 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+, potent antibacterial activity
0.0154
curcumin
Helicobacter pylori
Q56S04
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
0.0035
maesaquinone diacetate
Helicobacter pylori
Q56S04
IC50: 0.0035 mM, noncompetitive inhibition with respect to shikimate and NADP+
0.0098
epigallocatechin gallate
Toxoplasma gondii
-
pH 8.8, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.68
recombinant CEN.PK-aroE strain expressing the enzyme from Eschericha coli, pH 7.0, 25°C
184
-
after treatment with benzo-thiadiaziole-7-carbothioic acid S-methyl ester; pH 9.0, 25°C, fruits after harvest
732
additional information
additional information
-
during storage at 1°C, SKDH activity increases in all strawberries
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
8.5
8.8
9
shikimate dehydrogenase assay at, gallate production; shikimate dehydrogenase assay at, gallate production; shikimate dehydrogenase assay at, gallate production
10
7
shikimate dehydrogenase assay at, 3-dehydroshikimate production; shikimate dehydrogenase assay at, 3-dehydroshikimate production; shikimate dehydrogenase assay at, 3-dehydroshikimate production; shikimate dehydrogenase assay at, 3-dehydroshikimate production
8.8
assay at; assay at; assay at; assay at
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
at pH 7.0, the forward reaction catalyzed by Corynebacterium glutamicum SDH proceeds at a rate about 10fold faster than the reverse reaction
8.5 - 10.5
-
pH 8.5: about 50% of activity maximum, pH 10.5: about 90% of activity maximum
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
50