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(3E)-3-[2-(4-bromophenyl)hydrazinylidene]piperidine-2,4,6-trione
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(3R,3'R,4S,4'S,5R,5'R)-N,N'-(butane-1,4-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
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(3R,3'R,4S,4'S,5R,5'R)-N,N'-(ethane-1,2-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
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(3R,3'R,4S,4'S,5R,5'R)-N,N'-(propane-1,3-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
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(3R,4S,5R)-3,4,5-trihydroxy-N-(3-hydroxypropyl)cyclohex-1-ene-1-carboxamide
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(3R,4S,5R)-3,4,5-trihydroxy-N-(4-hydroxybutyl)cyclohex-1-ene-1-carboxamide
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(3R,4S,5R)-3,4,5-trihydroxy-N-(5-hydroxypentyl)cyclohex-1-ene-1-carboxamide
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(3R,4S,5R)-3,4,5-trihydroxy-N-(6-hydroxyhexyl)cyclohex-1-ene-1-carboxamide
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(3R,4S,5R)-3,4,5-tri[(tert-butyldimethylsilyl)oxy]cyclohex-1-enecarboxylic acid
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(4Z)-4-[2-(3-hydroxyphenyl)triazan-1-ylidene]-5-methyl-2-[(piperidin-1-yl)methyl]-2,4-dihydro-3H-pyrazol-3-one
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(azepan-1-yl)(3-methyl-4,5-dinitrophenyl)methanone
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1,2,4-triazolo[3,4-b][1,3,4]thiadiazole
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half-maximal inhibition at 0.023 mg/ml
1,3-benzodioxole-5-carbothioamide
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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
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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
2,2-bisepigallocatechin gallate
about 50% inhibition at 0.0025 mM
2,4-Dichlorophenoxyacetic acid
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2,5-dimethyl-1,4-phenylene bis(trifluoroacetate)
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2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3,5,7-triol
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2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4-oxo-4H-1-benzopyran-3-yl 6-deoxy-alpha-L-mannopyranoside
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2-(3,4-dihydroxyphenyl)ethyl 6-O-[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]-beta-D-glucopyranoside
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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
3,3,3-trifluoro-N-(2-nitrophenyl)-2-(trifluoromethyl)propanamide
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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
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3,5-dihydroxy-4-methylbenzoic acid
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3,5-Dihydroxybenzoate
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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-(3,4-dihydroxyphenyl)-2-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]propanoic acid
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3-(3-fluoropyridin-4-yl)-6-(phenoxymethyl)-1,2,4-triazolo[3,4-b]-1,3,4-thiadiazole
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3-(4-bromophenyl)-6-((2,4-dichlorophenoxy)methyl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
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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
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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
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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
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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
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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
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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
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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
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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
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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
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3-(4-fluorophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
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half-maximal inhibition at 0.0663 mg/ml
3-(4-hydroxyphenyl)-4-oxo-4H-1-benzopyran-7-yl hexopyranosiduronic acid
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3-(beta-naphthylmethyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
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half-maximal inhibition at 0.0407 mg/ml
3-ethyl-3,4-dihydro-2H-1-benzopyran
3-hydroxy-4-(methoxycarbonyl)-2,5-dimethylphenyl 3-formyl-2,4-dihydroxy-6-methylbenzoate
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3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexane-1-carboxylic acid
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4,4'-methylenebis(2,6-dibromo-3,5-dihydroxybenzoic acid)
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4-hydroxy-6-methyl-2-oxo-1-(2-phenylethyl)-1,2-dihydropyridine-3-carbaldehyde
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4-[(morpholin-4-yl)methyl]benzoic acid
4-[[(E)-(2-ethoxy-6-methyl-4-oxo-2H-1-benzopyran-3(4H)-ylidene)methyl]amino]-2-hydroxybenzoic acid
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5-(6-hydroxy-1-benzofuran-2-yl)-2-[(1E)-3-methylbut-1-en-1-yl]benzene-1,3-diol
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5-(hex-1-yn-1-yl)furan-2-carboxylic acid
5-[4-(1H-imidazol-2-ylcarbonyl)phenyl]thiophene-2-carboxylic acid
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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
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6-((2,4-dichlorophenoxy)methyl)-3-(3-fluoropyridin-4-yl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
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6-((4-bromophenoxy)methyl)-3-(4-bromophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
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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
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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
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half-maximal inhibition at 0.0277 mg/ml
6-(2,6-dichlorophenoxy) pyridin-3-amine
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60% inhibition at 0.4 mM
6-amino-1,2,3,4-tetrahydronaphthalen-1-one
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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-1-benzofuran-3(2H)-one
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6-hydroxy-2,3-dihydrobenzo[b]furan-3-one
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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
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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-1-benzopyran-4-one
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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
ajmalicine
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(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
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
cyclopropyl(5-hydroxy-1-benzofuran-3-yl)methanone
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32% inhibition at 0.4 mM
dianthrol
about 50% inhibition at 0.0025 mM
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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
epigallocatechin-3,5-digallate
about 50% inhibition at 0.0025 mM
epitheaflavin monogallate
about 50% inhibition at 0.0025 mM
ethyl 5-(1H-pyrazol-3-yl)thiophene-2-carboxylate
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28% inhibition at 0.4 mM
HgCl2
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complete inhibition at concentration 0.05 mM
hydroquinone
lower inhibitry potency, about 25% inhibition at 0.0025 mM
limonin
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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
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
N-methyl-N-(quinolin-6-ylmethyl)amine
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63% inhibition at 0.4 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
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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
p-hydroxymercuribenzoate
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moderate
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
quercetin
about 25% inhibition at 0.0025 mM
SDS
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nearly complete inactivation of AroE at 0.02%
strictamin
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akuammilan-17-oic acid methyl ester, from Alstonia scholaris leaves, interacting residues are Tyr129, Gln126, and Leu125
taxifolin
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'-bithiophene]-5-carboxylic acid
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[2-[2-(dimethylamino)ethoxy]phenyl]methanol
[4-(4-methylperhydro-1,4-diazepin-1-yl)phenyl]methanol
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67% inhibition at 0.4 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
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31% inhibition at 0.2 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
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31% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
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49% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
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49% inhibition at 0.2 mM
3-ethyl-3,4-dihydro-2H-1-benzopyran
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31% inhibition at 0.2 mM
3-ethyl-3,4-dihydro-2H-1-benzopyran
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31% inhibition at 0.2 mM
4-[(morpholin-4-yl)methyl]benzoic acid
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31% inhibition at 0.2 mM
4-[(morpholin-4-yl)methyl]benzoic acid
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31% inhibition at 0.2 mM
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
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29% inhibition at 0.2 mM
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
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29% inhibition at 0.2 mM
Cu2+
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curcumin
IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
curcumin
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a noncompetitive inhibitor
epicatechin gallate
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epicatechin gallate
over 75% inhibition at 0.0025 mM
epigallocatechin gallate
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epigallocatechin gallate
over 75% inhibition at 0.0025 mM
epigallocatechin gallate
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-
Hg2+
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iodoacetate
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methyl 3-hydroxy-1-benzothiophene-2-carboxylate
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33% inhibition at 0.2 mM
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
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33% inhibition at 0.2 mM
p-chloromercuribenzoate
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p-chloromercuribenzoate
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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
p-chloromercuribenzoate
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p-chloromercuribenzoate
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p-chloromercuribenzoate
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p-chloromercuribenzoate
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protocatechuic acid
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competitive inhibition
protocatechuic acid
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moderate
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
Zn2+
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-
[2-[2-(dimethylamino)ethoxy]phenyl]methanol
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45% inhibition at 0.2 mM
[2-[2-(dimethylamino)ethoxy]phenyl]methanol
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45% inhibition at 0.2 mM
additional information
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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
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additional information
screening for polyphenolc enzyme inhibitors, overview
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additional information
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screening for polyphenolc enzyme inhibitors, overview
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additional information
not inhibitory: quinate; not inhibitory: quinate
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additional information
not inhibitory: quinate; not inhibitory: quinate
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additional information
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not inhibitory: quinate; not inhibitory: quinate
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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
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additional information
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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
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additional information
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no inhibition of paralogue HI0607 by EDTA
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additional information
antibacterial activity of inhibitors, overview
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additional information
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antibacterial activity of inhibitors, overview
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additional information
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inhibitor screening
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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
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additional information
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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
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additional information
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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
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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
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additional information
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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
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additional information
screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
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additional information
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screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
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additional information
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structure-based inhibitor design, small-molecule library screening, inhibition mechanism analysis
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additional information
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no inhibition by curcumin
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