Information on EC 1.1.1.25 - shikimate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.25
-
RECOMMENDED NAME
GeneOntology No.
shikimate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
chorismate metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Metabolic pathways
-
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Biosynthesis of secondary metabolites
-
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Biosynthesis of antibiotics
-
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chorismate biosynthesis from 3-dehydroquinate
-
-
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9026-87-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
Uniprot
Manually annotated by BRENDA team
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bambusa sp.
bamboo
-
-
Manually annotated by BRENDA team
tea plant
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain IFO 3244
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-
Manually annotated by BRENDA team
strain IFO 3244
-
-
Manually annotated by BRENDA team
gene aroE; strain SS1, gene aroE
SwissProt
Manually annotated by BRENDA team
multienzyme complex
-
-
Manually annotated by BRENDA team
no activity in Homo sapiens
-
-
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Manually annotated by BRENDA team
enzyme complex of EC 4.2.1.10 and EC 1.1.1.25
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-
Manually annotated by BRENDA team
trees in Dabrowa Forest District, Pniewy Forest Division, re­gional directorate of state forests in Poznan, Poland
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-
Manually annotated by BRENDA team
pea
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-
Manually annotated by BRENDA team
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
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-
Manually annotated by BRENDA team
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
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Manually annotated by BRENDA team
homolog ael1; strain KT2240
UniProt
Manually annotated by BRENDA team
tomato
-
-
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
3-dehydroquinate + NADH + H+
quinate + NAD+
show the reaction diagram
3-dehydroquinate + NADPH + H+
quinate + NADP+
show the reaction diagram
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
show the reaction diagram
3-dehydroshikimate + NADH
shikimate + NAD+
show the reaction diagram
-
SDH reaction, very low activity with NAD+
-
-
r
3-dehydroshikimate + NADH + H+
shikimate + NAD+
show the reaction diagram
3-dehydroshikimate + NADPH
?
show the reaction diagram
3-dehydroshikimate + NADPH
shikimate + NADP+
show the reaction diagram
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
show the reaction diagram
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
show the reaction diagram
-
-
-
r
quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
show the reaction diagram
-
-
-
?
quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
quinate + NADP+
3-dehydroquinate + NADPH + H+
show the reaction diagram
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
show the reaction diagram
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
shikimate + NADP+
3-dehydroshikimate + NADPH
show the reaction diagram
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
show the reaction diagram
3-dehydroshikimate + NADPH
?
show the reaction diagram
3-dehydroshikimate + NADPH
shikimate + NADP+
show the reaction diagram
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
show the reaction diagram
P95001
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
show the reaction diagram
Q6PUF9, Q6PUG0
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
Q88GF6, Q88IJ7, Q88JP1, Q88K85, Q88RQ5
the fourth enzyme in the shikimate pathway
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
show the reaction diagram
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reversible activity of YdiB, no activity with paralogue HI0607
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-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,4-triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.023 mg/ml
2,2'-bithiophene-5-carboxylic acid
-
the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
-
2,2-bisepigallocatechin gallate
about 50% inhibition at 0.0025 mM
-
2,4-Dichlorophenoxyacetic acid
-
-
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
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
3,5-Dihydroxybenzoate
-
moderate
3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate
IC50: 0.0039 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+
3-(3-fluoropyridin-4-yl)-6-(phenoxymethyl)-1,2,4-triazolo[3,4-b]-1,3,4-thiadiazole
-
3-(4-bromophenyl)-6-((2,4-dichlorophenoxy)methyl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0396 mg/ml
3-(4-bromophenyl)-6-((2-methyl-4-chlorophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0216 mg/ml
3-(4-bromophenyl)-6-((4-chlorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0363 mg/ml
3-(4-bromophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0795 mg/ml
3-(4-bromophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0120 mg/ml
3-(4-bromophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0586 mg/ml
3-(4-chlorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.168 mg/ml
3-(4-chlorophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 5.052 mg/ml
3-(4-chlorophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.00937 mg/ml
3-(4-fluorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
3-(4-fluorophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0663 mg/ml
3-(beta-naphthylmethyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0407 mg/ml
3-ethyl-3,4-dihydro-2H-1-benzopyran
4-[(morpholin-4-yl)methyl]benzoic acid
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
6-((2,4-dichlorophenoxy)methyl)-3-(3-fluoropyridin-4-yl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
-
6-((4-bromophenoxy)methyl)-3-(4-bromophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0144 mg/ml
6-((4-bromophenoxy)methyl)-3-(4-chlorophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.00682 mg/ml
6-((4-fluorophenoxy)methyl)-3-(beta-naphthylmethyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
half-maximal inhibition at 0.0277 mg/ml
6-hydroxy-2,3-dihydrobenzo[b]furan-3-one
-
the inhibitor is identified by virtual screeening, 99% inhibition at 0.2 mM, mixed-type inhibition versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues
-
7-hydroxy-2,2,8-trimethyl-2,3-dihydro-4H-chromen-4-one
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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
-
arsenite
-
-
aurintricarboxylic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
baicalein
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
Cd2+
-
500 nM
curcumin
dianthrol
about 50% inhibition at 0.0025 mM
-
diethylenetriamine pentaacetic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
ebselen
lower inhibitry potency, about 25% inhibition at 0.0025 mM
ellagic acid
about 50% inhibition at 0.0025 mM
Epicatechin gallate
over 75% inhibition at 0.0025 mM
epigallocatechin gallate
epigallocatechin-3,5-digallate
about 50% inhibition at 0.0025 mM
epitheaflavin monogallate
about 50% inhibition at 0.0025 mM
guaiacol
-
-
HgCl2
-
complete inhibition at concentration 0.05 mM
hydroquinone
lower inhibitry potency, about 25% inhibition at 0.0025 mM
iodoacetate
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
Metal ions
-
-
-
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
N-ethylmaleimide
-
-
NADP+
product inhibition, competitive versus NADPH, noncompetitive versus 3-dehydroshikimate
nordihydroguaiaretic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
moderate
protocatechuic acid
Purpurogallin
about 50% inhibition at 0.0025 mM
pyridoxine
lower inhibitry potency, about 25% inhibition at 0.0025 mM
pyrogallin
about 50% inhibition at 0.0025 mM
SDS
-
nearly complete inactivation of AroE at 0.02%
shikimate
taxifolin, quercetin
about 25% inhibition at 0.0025 mM
-
theaflavanin
about 25% inhibition at 0.0025 mM
-
theaflavin monogallate
about 50% inhibition at 0.0025 mM
theaflavin-3,3-digallate
about 25% inhibition at 0.0025 mM
-
[2-[2-(dimethylamino)ethoxy]phenyl]methanol
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
Nonidet P-40
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120-190% activity of AroE at 0.1-0.5%
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
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treatment of fruits
Triton X-100
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120-190% activity at 0.1-0.5%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00036 - 0.42
3-dehydroquinate
0.029 - 186
3-dehydroshikimate
0.572 - 11.4
NAD+
0.007 - 0.279
NADP+
0.01 - 0.034
NADPH
0.783 - 10.2
quinate
0.0046 - 46.6
shikimate
0.05 - 0.087
shikimic acid
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 114
3-dehydroquinate
0.078 - 329
3-dehydroshikimate
5.2 - 97.1
NAD+
0.008 - 399
NADP+
45 - 50
NADPH
0.16 - 61.9
quinate
0.013 - 428
shikimate
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.143 - 272
3-dehydroquinate
9.6 - 1700
3-dehydroshikimate
262 - 3430
NADP+
24 - 4500
NADPH
18 - 3620
shikimate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
kinetic study of the enzyme-inhibitor complexes
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029
2-([2-([2-([2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl)-1,3-benzothiazol-6-yl]amino)2-oxoethyl]sulfanyl)-N-(2-naphthyl)acetamide
Helicobacter pylori
Q56S04
IC50: 0.0029 mM, competitive inhibition with respect to shikimate, noncompetitive to NADP+, potent antibacterial activity
0.0039
3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate
Helicobacter pylori
Q56S04
IC50: 0.0039 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+
0.0134
butyl 2-([3-(2-naphthyloxy)4-oxo-2-(trifluoromethyl)4H-chromen-7-yl]oxy)propanoate
Helicobacter pylori
Q56S04
IC50: 0.0134 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+, potent antibacterial activity
0.0154
curcumin
Helicobacter pylori
Q56S04
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
0.0037
Epicatechin gallate
Pseudomonas putida
Q88RQ5
pH 8.8, 25°C, recombinant enzyme
0.003 - 0.0098
epigallocatechin gallate
0.0035
maesaquinone diacetate
Helicobacter pylori
Q56S04
IC50: 0.0035 mM, noncompetitive inhibition with respect to shikimate and NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.2
-
crude extract
3.5
-
crude extract
3.9
purified recombinant AroE
9.68
recombinant CEN.PK-aroE strain expressing the enzyme from Eschericha coli, pH 7.0, 25°C
14.1
-
11.8fold purified enzyme
19.9
pH 9.0, 25°C, recombinant enzyme
25.4
-
purified enzyme
95
-
value about, fruits without any treatment
184
-
after treatment with benzo-thiadiaziole-7-carbothioic acid S-methyl ester; pH 9.0, 25°C, fruits after harvest
826
-
purified recombinant AroE
1479
-
87°C, pH 7.3, cosubstrate NAD+
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
oxidation of shikimate
6
reduction of 3-dehydroquinate
6.8 - 7.2
formation of shikimate
7.5
-
assay at
7.5 - 9.8
-
paralogue HI0607
7.7
-
Tris-HCl acid buffer
8 - 9
oxidation reaction, recombinant His-tagged enzyme
9 - 9.4
formation of 3-dehydroshikimate
9
assay at; assay at
9
shikimate dehydrogenase assay at, gallate production; shikimate dehydrogenase assay at, gallate production; shikimate dehydrogenase assay at, gallate production
10.1
-
glycine-sodium hydroxide buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
-
6 - 11
-
no activity below and above
6.5 - 12.5
-
activity range, overview
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
24
-
assay at
35
-
assay at
60
oxidation reaction, recombinant His-tagged enzyme