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Information on EC 1.1.1.25 - shikimate dehydrogenase
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1.1.1.25 shikimate dehydrogenaseIUBMB Comments
NAD+ cannot replace NADP+ . In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase .
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Word Map
- 1.1.1.25
- 3-dehydroshikimate
- drug development
-
cinnamyl
-
5-enolpyruvylshikimate
-
pentafunctional
- dahp
-
ammonialyase
- 3-dehydroquinase
- agriculture
- analysis
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
3-dehydroquinate dehydratase/shikimate dehydrogenase, 5-dehydroshikimate reductase, ael1, Af2327, AroE, bifunctional dehydroquinate dehydratase-shikimate dehydrogenase, cgR_0495, cgR_1677, dehydroquinate dehydratase-shikimate dehydrogenase, dehydroquinate dehydratase/shikimate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-dehydroshikimate reductase
-
-
-
-
ael1
Af2327
AroE
bifunctional dehydroquinate dehydratase-shikimate dehydrogenase
-
cgR_0495
cgR_1677
dehydroquinate dehydratase/shikimate dehydrogenase
dehydroshikimic reductase
-
-
-
-
DHQ-SDH
DQD/SDH
NADP-dependent shikimate dehydrogenase
Poptr1
Poptr5
qsuD
rifI
SD
SDH
sdhL
shikimate 5-dehydrogenase
shikimate dehydrogenase
shikimate oxidoreductase
-
-
-
-
shikimate:NADP oxidoreductase
-
-
-
-
shikimate:NADP+ 5-oxidoreductase
-
-
-
-
SKDH
tm0346
additional information
shikimate 5-dehydrogenase
-
-
-
-
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
-
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 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
-
-
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-
redox reaction
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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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 + 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 + 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 + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH
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assay at 24°C, pH 9.0
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-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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analysis of the 3-dehydroshikimate binding site
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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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+
A0A1K3RIC7
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-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A1K3RIC7
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-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A1K3RIC7
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
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-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
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-
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
?
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the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities
-
-
?
additional information
?
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
-
-
?
additional information
?
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
-
-
?
additional information
?
-
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
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?
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
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-
?
additional information
?
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-
fourth enzyme in the shikimate biosynthetic pathway
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?
additional information
?
-
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the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
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?
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
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-
?
additional information
?
-
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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
?
-
-
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
-
-
?
additional information
?
-
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
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)+
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 + NADPH
?
-
pathway of biosynthesis of aromatic amino acids
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
the fourth enzyme in the shikimate pathway
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
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+
A0A1K3RIC7
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A1K3RIC7
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
A0A1K3RIC7
-
-
-
?
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
?
-
-
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 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 (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
-
-
?
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 (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
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
-
additional information
NADH shows about 2% of the activity with NADPH
-
additional information
-
NADH shows about 2% of the activity with NADPH
-
additional information
NADPH shows about 2.5% of the activity with NADPH
-
additional information
NADPH shows about 2.5% of the activity with NADPH
-
additional information
-
NADPH shows about 2.5% of the activity with NADPH
-
additional information
cofactor binding might trigger domain movement
-
additional information
-
for Poptr5, no activity with shikimate is detectable in the presence of NAD+ even with elevated enzyme concentrations
-
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2,4-triazolo[3,4-b][1,3,4]thiadiazole
A0A1K3RIC7
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-([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
A0A1K3RIC7
-
3-(4-bromophenyl)-6-((2,4-dichlorophenoxy)methyl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
-
3-(4-fluorophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
-
6-((4-bromophenoxy)methyl)-3-(4-bromophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
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
A0A1K3RIC7
31% inhibition at 0.2 mM
4-[(morpholin-4-yl)methyl]benzoic acid
A0A1K3RIC7
31% inhibition at 0.2 mM
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
A0A1K3RIC7
29% inhibition at 0.2 mM
curcumin
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
epicatechin gallate
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epigallocatechin gallate
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
A0A1K3RIC7
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
A0A1K3RIC7
45% inhibition at 0.2 mM
additional information
screening for polyphenolc enzyme inhibitors, overview
-
additional information
-
screening for polyphenolc enzyme inhibitors, overview
-
additional information
not inhibitory: quinate; not inhibitory: quinate
-
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
A0A1K3RIC7
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Differential responses of five cherry tomato varieties to water stress: Changes on phenolic metabolites and related enzymes.
Tuberculosis
Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Expression, purification and properties of shikimate dehydrogenase from Mycobacterium tuberculosis.
Tuberculosis
Functional shikimate dehydrogenase from Mycobacterium tuberculosis H37Rv: purification and characterization.
Tuberculosis
Homogeneous recombinant Mycobacterium tuberculosis shikimate dehydrogenase production: an essential step towards target-based drug design.
Tuberculosis
In silico identification of potential inhibitors against shikimate dehydrogenase through virtual screening and toxicity studies for the treatment of tuberculosis.
Tuberculosis
Kinetic and chemical mechanisms of shikimate dehydrogenase from Mycobacterium tuberculosis.
Tuberculosis
Simulations of Shikimate Dehydrogenase from Mycobacterium tuberculosis in Complex with 3-Dehydroshikimate and NADPH Suggest Strategies for MtbSDH Inhibition.
Tuberculosis
Structural studies of shikimate 5-dehydrogenase from Mycobacterium tuberculosis.
Tuberculosis
The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase.
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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
0.321
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
-
Michaelis-Menten kinetics
-
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
-
steady-state kinetics of recombinant AroE
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
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
-
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+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
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
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
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
IC50: 0.0134 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+, potent antibacterial activity
0.0154
curcumin
Helicobacter pylori
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
0.0035
maesaquinone diacetate
Helicobacter pylori
IC50: 0.0035 mM, noncompetitive inhibition with respect to shikimate and NADP+
0.002
epicatechin gallate
Arabidopsis thaliana
pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
0.0021
epigallocatechin gallate
Arabidopsis thaliana
pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
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
184
732
9.68
recombinant CEN.PK-aroE strain expressing the enzyme from Eschericha coli, pH 7.0, 25°C
additional information
184
-
after treatment with benzo-thiadiaziole-7-carbothioic acid S-methyl ester
additional information
-
during storage at 1°C, SKDH activity increases in all strawberries
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
7.3
8.5
8.8
7
shikimate dehydrogenase assay at, 3-dehydroshikimate production
9
shikimate dehydrogenase assay at, gallate production
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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
87