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Information on EC 1.1.1.25 - shikimate dehydrogenase (NADP+)
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1.1.1.25 shikimate dehydrogenase (NADP+)IUBMB 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 . cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
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Word Map
- 1.1.1.25
- 3-dehydroshikimate
- drug development
-
subdural
-
cinnamyl
- dahps
-
5-enolpyruvylshikimate
-
pentafunctional
- 3-dehydroquinase
-
ammonialyase
- analysis
- diagnostics
- food industry
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-dehydroquinate dehydratase/shikimate dehydrogenase, 5-dehydroshikimate reductase, 5-dehydroshikimic reductase, ael1, Af2327, AroE, bifunctional dehydroquinate dehydratase-shikimate dehydrogenase, bifunctional DHQD-SDH/QDH, cgR_0495, cgR_1677, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-dehydroquinate dehydratase/shikimate dehydrogenase
5-dehydroshikimate reductase
-
-
-
-
5-dehydroshikimic reductase
-
-
-
-
ael1
Af2327
AroE
bifunctional dehydroquinate dehydratase-shikimate dehydrogenase
-
cgR_0495
cgR_1677
dehydroquinate dehydratase/shikimate dehydrogenase
dehydroshikimic reductase
-
-
-
-
DHQ-SDH
DHS reductase
-
-
-
-
DQD/SDH
HpSDH
NAD+-dependent enzyme quinate/shikimate dehydrogenase
NADP-dependent shikimate dehydrogenase
Poptr1
Poptr5
qsuD
quinate/shikimate dehydrogenase
rifI
SD
SDH
sdhL
shikimate 5-dehydrogenase
shikimate dehydrogenase
shikimate oxidoreductase
-
-
-
-
shikimate:NADP oxidoreductase
-
-
-
-
shikimate:NADP+ 5-oxidoreductase
-
-
-
-
shikimate:NADP+ oxidoreductase
-
-
-
-
SKDH
tm0346
YdiB
additional information
dehydroquinate dehydratase/shikimate dehydrogenase
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
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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]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
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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 + NADP+
gallate + NADPH + H+
-
-
-
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
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
activity of T381 enzyme mutants, not of wild-type enzyme, see also EC 1.1.1.282
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
activity by only mutant S275G/T318G, not the wild-type enzyme
-
-
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+
-
the enzyme is also active with NAD+
-
-
r
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
-
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+
-
-
-
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+
-
-
-
-
r
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
?
-
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
-
-
?
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
?
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
additional information
?
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
additional information
?
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
additional information
?
-
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
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
?
-
-
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 wild-type enzyme PoptrSDH1 is highly shikimate-specific, only the S275G/T318G mutant shows activity with quinate
-
-
-
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
?
-
analyzing the catalytic activity of SDH, the enzyme produce shikimate from 3-dehydroshikimate (3-DHS) in the presence of NADPH as a cofactor, whereas it forms gallic acid in the presence of NADP+
-
-
-
additional information
?
-
-
analyzing the catalytic activity of SDH, the enzyme produce shikimate from 3-dehydroshikimate (3-DHS) in the presence of NADPH as a cofactor, whereas it forms gallic acid in the presence of NADP+
-
-
-
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
3-dehydroshikimate + NADP+
gallate + NADPH + H+
-
-
-
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)+
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+
-
the enzyme is also active with NAD+
-
-
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+
-
-
-
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+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
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
NADPH
enzyme MtbSDH utilizes NADPH in the proS form, binding structure, overview
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
(3E)-3-[2-(4-bromophenyl)hydrazinylidene]piperidine-2,4,6-trione
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(butane-1,4-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(ethane-1,2-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(propane-1,3-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(3-hydroxypropyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(4-hydroxybutyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(5-hydroxypentyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(6-hydroxyhexyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-tri[(tert-butyldimethylsilyl)oxy]cyclohex-1-enecarboxylic acid
-
(4Z)-4-[2-(3-hydroxyphenyl)triazan-1-ylidene]-5-methyl-2-[(piperidin-1-yl)methyl]-2,4-dihydro-3H-pyrazol-3-one
-
1,2,4-triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.023 mg/ml
1,3-benzodioxole-5-carbothioamide
-
the compound shows higher affinity for the shikimate binding site than for the NADP+ binding site, mixed full inhibition mechanism versus shikimate, non-competitive full inhibition mechanism versus NADP+, interaction analysis and enzyme-bound structure, overview. 75% inhibition at 0.4 mM
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-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4-oxo-4H-1-benzopyran-3-yl 6-deoxy-alpha-L-mannopyranoside
-
2-(3,4-dihydroxyphenyl)ethyl 6-O-[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]-beta-D-glucopyranoside
-
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
3,3,3-trifluoro-N-(2-nitrophenyl)-2-(trifluoromethyl)propanamide
-
3,5,7-trihydroxy-3'-(4-hydroxy-3-methoxyphenyl)-2'-(hydroxymethyl)-2,3,3',4'-tetrahydro-2'H,4H-[2,6'-bi-1-benzopyran]-4-one
-
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-(3,4-dihydroxyphenyl)-2-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]propanoic acid
-
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-(4-hydroxyphenyl)-4-oxo-4H-1-benzopyran-7-yl hexopyranosiduronic acid
-
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
3-hydroxy-4-(methoxycarbonyl)-2,5-dimethylphenyl 3-formyl-2,4-dihydroxy-6-methylbenzoate
-
3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
4-hydroxy-6-methyl-2-oxo-1-(2-phenylethyl)-1,2-dihydropyridine-3-carbaldehyde
-
4-[[(E)-(2-ethoxy-6-methyl-4-oxo-2H-1-benzopyran-3(4H)-ylidene)methyl]amino]-2-hydroxybenzoic acid
-
5-(6-hydroxy-1-benzofuran-2-yl)-2-[(1E)-3-methylbut-1-en-1-yl]benzene-1,3-diol
-
5-[4-(1H-imidazol-2-ylcarbonyl)phenyl]thiophene-2-carboxylic acid
-
the compound shows higher affinity for the shikimate binding site than for the NADP+ binding site, uncompetitive full inhibition versus shikimate and mixed full inhibition versus NADP+, interaction analysis and enzyme-bound structure, overview. 98% inhibition at 0.4 mM
5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-2,2-dimethyl-1,3-dioxane-4,6-dione
-
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-amino-1,2,3,4-tetrahydronaphthalen-1-one
-
the compound presents a higher affinity for NADP+ binding site than for shikimate binding, mixed partial inhibition mechanism versus NADP+ and mixed full versus shikimate, interaction analysis and enzyme-bound structure, overview. 91% inhibition at 0.4 m
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
6-hydroxy-7-methyl-1-benzofuran-3(2H)-one
-
mixed partial inhibition mechanism versus NADP+ and shikimate, interaction analysis and enzyme bound structure, overview. 98% inhibition at 0.4 mM
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
ajmalicine
-
(19alpha)-16,17-didehydro-19-methyloxayohimban-16-carboxylic acid methyl ester, from Rauwolfia serpentina leaves and roots, interacting residues are Asp131 and Arg130
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
cyclopropyl(5-hydroxy-1-benzofuran-3-yl)methanone
-
32% inhibition at 0.4 mM
diethylenetriamine pentaacetic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
ethyl 5-(1H-pyrazol-3-yl)thiophene-2-carboxylate
-
28% inhibition at 0.4 mM
hydroquinone
lower inhibitry potency, about 25% inhibition at 0.0025 mM
limonin
-
7,16-dioxo-7,16-dideoxylimondiol, from Citrus sp. fruits, interacting residues are Thr75, Thr78, Val71, Gln101, and Pro103
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
N-[2,2-dimethyl-6-(1-methyldioxidan-1-ium-1-yl)-3,4-dihydro-2H-1-benzopyran-4-yl]-N2-methyl-N2-[(pyridin-2-yl)methyl]glycinamide
-
34% inhibition at 0.4 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
strictamin
-
akuammilan-17-oic acid methyl ester, from Alstonia scholaris leaves, interacting residues are Tyr129, Gln126, and Leu125
[4-(4-methylperhydro-1,4-diazepin-1-yl)phenyl]methanol
-
67% inhibition at 0.4 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
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+
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
-
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
-
ten clinical isolates of Acinetobacter baumannii are used for inhibitor screening. Ajmalicine, strictamin, and limonin exhibit promising binding towards multiple drug targets of Acinetobacter baumannii in comparison with the binding between standard drugs and their targets. The tested isolates exhibit resistance to antibiotics clinafloxacin, imipenem and polymyxin-E, and the herbal preparations (crude extracts) demonstrate a significant antibacterial potential. Docking study and molecular dynamic simulations, model refinement and validation, overview. Acinetobacter baumannii exhibits resistance to a broad range of antibiotics due to the presence of a protective capsule, lipopolysaccharide, AbaR resistance islands, OmpA, efflux pumps, biofilms formation, and other mechanisms. Evaluation of drug targets in Acinetobacter baumannii. The toxicity prediction for ajmalicine (Rauvolfia serpentina) and strictamin (Alstonia scholaris) are predicted to be non-carcinogenic in both mouse and rat models making them potential leads
-
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
synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli, evaluation for in vitro SDH inhibition and antibacterial activity against Escherichia coli, molecular docking studies, overview. All tested compounds are mixed-type inhibitors, diamide derivatives display more inhibitory activity than synthesised monoamides
-
additional information
-
synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli, evaluation for in vitro SDH inhibition and antibacterial activity against Escherichia coli, molecular docking studies, overview. All tested compounds are mixed-type inhibitors, diamide derivatives display more inhibitory activity than synthesised monoamides
-
additional information
antibacterial activity of inhibitors, overview
-
additional information
-
antibacterial activity of inhibitors, overview
-
additional information
integrated virtual screening/molecular docking-based virtual screening, and antibacterial test for identification of enzyme inhibitors, screening of ZINC database. The HpSDH active site prefers to accommodate amphipathic and polar inhibitors that consist of an aromatic core as well as a number of oxygen-rich polar/charged substituents such as hydroxyl, carbonyl, and carboxyl groups. Subpockets 1- and 2-specific inhibitors exhibit a generally higher activity than subpocket 3-specific inhibitors. Molecular dynamics simulations revealed an intense nonbonded network of hydrogen bonds, Pi-Pi stacking, and van der Waals contacts at the tightly packed complex interfaces of active-site subpockets with their cognate inhibitors, conferring strong stability and specificity to these complex systems. Binding energetic analysis demonstrates that the identified potent inhibitors can target their cognate subpockets with an effective selectivity over noncognate ones. Determination of MIC values of the compounds against Helicobacter strains ATCC43504 and ATCC700392, and structural and energetic analysis of subpocket-inhibitor interactions, overview
-
additional information
-
integrated virtual screening/molecular docking-based virtual screening, and antibacterial test for identification of enzyme inhibitors, screening of ZINC database. The HpSDH active site prefers to accommodate amphipathic and polar inhibitors that consist of an aromatic core as well as a number of oxygen-rich polar/charged substituents such as hydroxyl, carbonyl, and carboxyl groups. Subpockets 1- and 2-specific inhibitors exhibit a generally higher activity than subpocket 3-specific inhibitors. Molecular dynamics simulations revealed an intense nonbonded network of hydrogen bonds, Pi-Pi stacking, and van der Waals contacts at the tightly packed complex interfaces of active-site subpockets with their cognate inhibitors, conferring strong stability and specificity to these complex systems. Binding energetic analysis demonstrates that the identified potent inhibitors can target their cognate subpockets with an effective selectivity over noncognate ones. Determination of MIC values of the compounds against Helicobacter strains ATCC43504 and ATCC700392, and structural and energetic analysis of subpocket-inhibitor interactions, 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
simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH for MtbSDH inhibition strategy, overview. Rational design of hybrid MtbSDH inhibitors able to bind in both the substrate (DHS) and cofactor (NADPH) pockets
-
additional information
-
simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH for MtbSDH inhibition strategy, overview. Rational design of hybrid MtbSDH inhibitors able to bind in both the substrate (DHS) and cofactor (NADPH) pockets
-
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
-
additional information
-
structure-based inhibitor design, small-molecule library screening, inhibition mechanism analysis
-
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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
Brain Injuries, Traumatic
A review of sub acute subdural hematoma (SASDH) with our institutional experience and its management by double barrel technique (DbT): A novel technique.
Dehydration
Differential responses of five cherry tomato varieties to water stress: Changes on phenolic metabolites and related enzymes.
Hypersensitivity, Delayed
The pathogenesis of subacute subdural hematoma: A report of 3 cases and literature review.
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.
Tuberculosis
Theoretical characterization of the shikimate 5-dehydrogenase reaction from Mycobacterium tuberculosis by hybrid QC/MM simulations and quantum chemical descriptors.
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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
0.287
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
0.322
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH2, DQD activity
0.331
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
0.381
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.449
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
0.466
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.878
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
0.882
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH3, DQD activity
8.83
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
9.44
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
30.6
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
186
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH4
2.351
L-quinate
-
mutant S275G/T318G, pH and temperature not specified in the publication
3.33
L-quinate
pH and temperature not specified in the publication, mutant T381G
4.075
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
4.485
L-quinate
pH and temperature not specified in the publication, mutant T381S
5.135
L-quinate
pH and temperature not specified in the publication, mutant T381A
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
0.0415
NADP+
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
0.0426
NADP+
-
pH not specified in the publication, 25°C, with shikimate
0.046
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate
0.0538
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.0565
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.0652
NADP+
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
0.112
NADP+
pH 8.8, presence of 2 mM shikimate
0.114
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.115
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate
0.138
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate
0.217
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.00438
NADPH
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
0.0231
NADPH
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
0.0495
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.249
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate
0.267
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate
0.27
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate
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
0.0326
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
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+
0.12
shikimate
-
pH and temperature not specified in the publication
0.1468
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.155
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.2
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.223
shikimate
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.273
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
0.279
shikimate
-
pH and temperature not specified in the publication
0.321
shikimate
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.346
shikimate
-
with NAD+, 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
0.427
shikimate
-
with NAD+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.548
shikimate
pH and temperature not specified in the publication, mutant S338G
0.604
shikimate
pH and temperature not specified in the publication, wild-type enzyme
0.611
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.685
shikimate
-
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
0.882
shikimate
pH and temperature not specified in the publication, mutant S338G/T381G
1.539
shikimate
pH and temperature not specified in the publication, mutant T381S
1.613
shikimate
pH and temperature not specified in the publication, mutant T381G
2.05
shikimate
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
2.512
shikimate
pH and temperature not specified in the publication, mutant T381A
3.64
shikimate
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
4.2
shikimate
pH 8.8, presence of 2 mM NAD+
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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
0.046
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.168
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
0.405
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
2.14
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
2.87
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
3.67
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
8.62
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
30.9
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
47
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH1, shikimate formation
57.6
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
60.4
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
95.85
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
307
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.062
L-quinate
pH and temperature not specified in the publication, mutant T381S
0.113
L-quinate
pH and temperature not specified in the publication, mutant T381A
6.7
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
8.8
L-quinate
pH and temperature not specified in the publication, mutant T381G
5.2
NAD+
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