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(1R,2S,3S,5S,7S)-10-hydroxy-3-oxo-2-oxa-5-azatricyclo[4.3.1.1(4,8)]undecane-8-carboxylate
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
(1R,3R,5S,8R)-2-azatricyclo[3.3.1.0(1,8)]-non-6-ene-3,5-dicarboxylate
-
exo arizidine analogue, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
(1R,3R,5S,8R)-8-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
(1R,3R,5S,8R)-8-hydroxy-5-nitro-2-azabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
(1R,3R,5S,8R)-8-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
(1R,3R,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
(1R,3S,5S,8R)-8-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
(1R,3S,5S,8R)-8-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
(1R,3S,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
(1R,3S,6S,8S,10S)-10-hydroxy-4-oxo-5-oxa-2-azatricyclo[4.3.1.13,8]undecane-8-carboxylic acid
-
(1R,5R,8R)-8-hydroxy-2-oxabicyclo[3.3.1]nona-3,6-diene-3,5-dicarboxylic acid
-
(1R,5S,8R)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
(1S,2aR,2bR,3S)-4-oxohexahydro-1H-5-oxa-2b-aza-1,3-methanocyclopropa[cd]indene-1-carboxylic acid
-
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
(1S,3S,5R,6R)-6-hydroxy-4-oxabicyclo[3.3.1]non-7-ene-1,3-dicarboxylate
endo-oxabicyclic dicarboxylic acid is a good geometric mimic of transition state
(1S,4S,6R,8S,10S)-3-oxo-5-aza-2-oxa-tetracyclo[4.3.1.(4,8).0(6,10)]undecane-8-carboxylate
-
tetracyclic lactone, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
(2E)-8-exo-3-Hydroximino-8-hydroxy-2-oxabicyclo-[3.3.1]non-6-ene-5-carboxylic acid
-
poor
(2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid
-
(2Z)-2-(4-chlorophenyl)-3-[4-(dimethoxymethyl)-2-nitrophenyl]prop-2-enoic acid
competitive
(3R,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
(3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
(3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
(Z)-3-((5-nitrothiazol-2-yl)imino)indolin-2-one
-
-
(Z)-3-((6-nitrobenzo[d]thiazol-2-yl)imino)indolin-2-one
-
-
(Z)-3-(4-nitrobenzylidene)indolin-2-one
MIC is 0.0235 mM
(Z)-3-(hydroxyimino)indolin-2-one
-
-
(Z)-N-(1-acetyl-2-oxoindolin-3-ylidene)hydrazinecarbothioamide
-
-
(Z)-N-(1-acetyl-2-oxoindolin-3-ylidene)hydrazinecarboxamide
-
-
(Z)-N-(2-oxoindolin-3-ylidene)hydrazinecarbothioamide
-
-
(Z)-N-(2-oxoindolin-3-ylidene)hydrazinecarboxamide
-
-
1-(2-(tert-butyl)-5-chloro-7-(methylsulfonyl)-1H-indol-3-yl)ethan-1-one
45% inhibition at 0.03 mM
1-(prop-1-en-2-yl)indoline-2,3-dione
-
-
1-acetylindoline-2,3-dione
-
-
1-ethylindoline-2,3-dione
-
-
1-isopropyl-2-methoxy-4-methylbenzene
-
1-isopropylindoline-2,3-dione
-
-
1-methylindoline-2,3-dione
-
-
1-phenylindoline-2,3-dione
-
-
1-pivaloylindoline-2,3-dione
-
-
1-Substituted adamantane derivatives
-
order of decreasing inhibitory activity with the various substituents: -PO32-, -P(OCH3)O2, CO2-, -CH2CO2-, -SO2-,Y -SO3-
2-(1-Carboxy-1,4-dihydrobenzyl)acrylic acid
-
-
2-chloro-3-(5,6-difluoro-1H-indol-3-yl)quinoxaline
2-chloro-4-(ethoxycarbonyl)-1-hydroxy-6-methylquinolin-1-ium
-
2-isopropyl-5-methylphenyl acetate
-
2-methyl-5-(prop-1-en-2-yl)cyclohexanol
-
2-[2-[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]ethyl]-4-methylpentanoic acid
competitive
3-((5-nitrothiophen-2-yl)methylene)indolin-2-one
-
-
3-((dihydroxyamino)thio)-4-((3,5-dimethoxyphenethyl)amino)-5-nitrobenzoic acid
competitive
3-(3-methoxyphenyl)-5,6,7,8-tetrahydrobenzo[b]thieno[2,3d]pyrimidin-4[3H]-one
3-(4-nitrobenzylidene)indolin-2-one
-
-
3-amino-1-(3-(4-hydroxybut-1-yn-1-yl)phenyl)-1H-benzol[f]chromene-2-carbonitril
3-Chloroadamantane-1-acetic acid
-
-
3-endo,6-exo-6-Hydroxy-7-bicyclo[3.3.1]-nonene-1,3-dicarboxylic acid
-
poor
3-endo,8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
potent
3-methyl-5-(propan-2-yl)phenol
-
4-(3,4-dimethoxyphenethylamino)-3-nitro-5-sulfamoylbenzoic acid
4-Methyl-DL-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-(2,3-dichlorophenyl)indoline-2,3-dione
-
-
5-(2,5-dimethylphenyl)indoline-2,3-dione
-
-
5-(4-(3-(tert-butyl)phenyl)piperazin-1-yl)indoline-2,3-dione
-
-
5-(4-(furan-2-carbonyl)piperazin-1-yl)indoline-2,3-dione
-
-
5-(4-methylpiperazin-1-yl)indoline-2,3-dione
-
-
5-(piperazin-1-yl)indoline-2,3-dione
-
-
5-(piperidin-1-yl)indoline-2,3-dione
-
-
5-isopropyl-2-methylaniline
-
5-naphthyl-7-propyl-3H-pyrazolo-[4,3-d][1,2,3]triazin-4[5h]-one
5-naphthyl-7-propyl-3H-pyrazolo[4,3-d][1,2,3]triazin-4(5H)-one
-
5-phenylindoline-2,3-dione
-
-
6'-iodo-1,3-dihydro-1'H-spiro[indene-2,2'-quinazolin]-4'(3'H)-one
a spiro 2,3-dihydroquinazolin-4(1H)-one
6,6'-dinitro-[1,1'-biphenyl]-2,2'-dicarboxylic acid
-
6-hydroxybicyclo[3.3.1]nonane-1,3-dicarboxylic acid
-
6-Methyl-DL-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]nona-3,6-diene-3,5-dicarboxylic acid
-
slight
8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
competitive inhibition
adamantan phosphonic acid
-
adamantane-1-carboxylic acid
-
adamantane-1-phosphonate
-
no inhibitory effect up to concentrations of 0.1 and 1 mM
DL-3-fluoro-Phe
-
enzyme form CM1 is inhibited, enzyme form CM2 not
DL-5-Fluoro-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
DL-5-hydroxy-Trp
-
enzyme form CM1 is inhibited, enzyme form CM2 not
endo-Oxabicylic transition state analogue inhibitor
-
-
-
ethyl 4-(2-(4-hydroxybut-1-yn-1-yl)phenyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
ferulic acid
-
inhibits enzyme form CM3
L-Trp
96% residual activity at 0.2 mM
methyl 4-(methylamino)-3-nitrobenzoate
N-(4-fluoro-2-(5-fluoro-1-(methylsulfonyl)-1H-inden-2-yl)phenyl)methanesulfonamide
-
N-[(3-(2-amino-3-cyano-2H-benzo[h]chromen-4-y))phenyl]methylidyne]-2-hydroxyethanaminium
-
N-[[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]carbonyl]leucine
-
NaCl
-
inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe
oxabicyclic dicarboxylic acid
transition state analogon, competitive inhibition
p-coumaric acid
-
inhibits enzyme form CM1, CM2 and CM3
phenylalanine
model of the AtCM1x02phenylalanine complex including residues Arg79-Val290 and Val307-Asp340, the phenylalanine ligand, and 83 waters, inhibits about 20fold
Transition state analogue inhibitor
-
-
-
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
-
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
-
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
2-chloro-3-(5,6-difluoro-1H-indol-3-yl)quinoxaline
-
2-chloro-3-(5,6-difluoro-1H-indol-3-yl)quinoxaline
-
-
3-(3-methoxyphenyl)-5,6,7,8-tetrahydrobenzo[b]thieno[2,3d]pyrimidin-4[3H]-one
-
3-(3-methoxyphenyl)-5,6,7,8-tetrahydrobenzo[b]thieno[2,3d]pyrimidin-4[3H]-one
-
-
3-amino-1-(3-(4-hydroxybut-1-yn-1-yl)phenyl)-1H-benzol[f]chromene-2-carbonitril
-
3-amino-1-(3-(4-hydroxybut-1-yn-1-yl)phenyl)-1H-benzol[f]chromene-2-carbonitril
-
-
4-(3,4-dimethoxyphenethylamino)-3-nitro-5-sulfamoylbenzoic acid
-
-
4-(3,4-dimethoxyphenethylamino)-3-nitro-5-sulfamoylbenzoic acid
-
5-naphthyl-7-propyl-3H-pyrazolo-[4,3-d][1,2,3]triazin-4[5h]-one
-
5-naphthyl-7-propyl-3H-pyrazolo-[4,3-d][1,2,3]triazin-4[5h]-one
-
-
Adamantane-1-acetic acid
-
-
Adamantane-1-acetic acid
-
caffeic acid
-
enzyme forms CM1 and CM2 are inhibited, enzyme form CM3 is unaffected
caffeic acid
-
enzyme form CM1 is inhibited
caffeic acid
-
enzyme form CM1 is inhibited
caffeic acid
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is inhibited
carvacrol
-
chlorogenic acid
CGA, a structural analogue of chorismic acid, is an inhibitor of chorismate mutase, type II regulatory domain (BsCM_2). It binds to BsCM_2 with a higher affinity than chorismate. Similar to BsCM_2, in BsAroH, the chlorogenic acid's position is shifted from the transition state analogue position. The chlorogenic acid interacts with residues Arg63, Val73, Thr74 from one chain and Arg7, Arg90, Val114, Leu115, and Arg116 from the adjacent chain; CGA, a structural analogue of chorismic acid, is an inhibitor of chorismate mutase, type II regulatory domain (BsCM_2). It binds to BsCM_2 with a higher affinity than chorismate. The BsCM_2-CGA structure has several residues in alternate conformations. His73 exists as alternative conformation in both the chains. At active site S1, the chlorogenic acid makes hydrogen bonds with the side chain of Arg27, Lys38, Gln86, and the main chain atoms of Arg45, Asp47, and Phe79 of chain B. The ligand molecule also interacts with Lys38, Arg50, and Lys80 of chain B, and Arg10 of chain A through water bridge formation. However, at active site S2, along with the above interactions, the ligand forms a direct hydrogen bond with Lys80 and an additional water bridge-mediated hydrogen bond with Gln86 of chain A
chlorogenic acid
-
enzyme forms CM1 and CM2 are inhibited, enzyme form CM3 is unaffected
chorismate
Q9Y7B2
-
chorismate
-
strain WB672, inhibition above 2 mM
Co2+
-
2 mM Co2+ decreases CM0819 activity by 52.4%
Cu2+
-
-
Fe2+
-
-
Hg2+
-
-
L-Phe
-
poor noncompetitive
L-Phe
-
plastidic isoenzyme is inhibited, cytosolic enzyme not
L-Phe
-
Trp reverses inhibition
L-Phe
-
55000 MW enzyme form. The 59000 MW enzyme form is not inhibited
L-Phe
-
chorismate mutase P is strongly inhibited, chorismate mutase T is not inhibited
L-Phe
-
enzyme form CM1 and CM3 are inhibited
L-Phe
28% residual activity at 0.2 mM
L-Phe
-
enzyme form CM1 is inhibited
L-Phe
-
enzyme form CM1 is inhibited; enzyme form CM3 is inhibited
L-Phe
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; enzyme form CM3 is inhibited
L-Phe
-
enzyme form CM1 is inhibited; Trp reverses inhibition
L-Phe
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited
L-tryptophan
-
allosteric inhibitor
L-tryptophan
-
allosteric. The Trp at the dimer interface interacts extensively with residues from both subunits. The unexpected gene duplication possibly leads to a different allosteric regulation mechanism than that is known for other CMs
L-Tyr
-
plastidic isoenzyme is inhibited, cytosolic enzyme not
L-Tyr
-
1.25 mM, 85% inhibition; Trp reverses inhibition
L-Tyr
-
55000 MW enzyme form. The 59000 MW enzyme form is not inhibited
L-Tyr
-
slight inhibition of chorismate mutase P and no inhibition of chorismate mutase T
L-Tyr
-
enzyme forms CM1 and CM3 are inhibited
L-Tyr
63% residual activity at 0.2 mM
L-Tyr
-
enzyme form CM1 is inhibited
L-Tyr
-
enzyme form CM1 is inhibited; enzyme form CM3 is inhibited
L-Tyr
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; enzyme form CM3 is inhibited
L-Tyr
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; Trp reverses inhibition
L-Tyr
-
wild-type enzyme is inhibited. Mutant enzymes with amino acid exchange at Thr234, especially Tyr234Phe, mutant enzyme Ile225Thr and Ile225Thr/Thr226Ile are insensitive
L-Tyr
-
enzyme form CM2 is not inhibited
methyl 4-(methylamino)-3-nitrobenzoate
-
methyl 4-(methylamino)-3-nitrobenzoate
competitive
Mn2+
-
2 mM Mn2+ decreases CM0819 activity by 38.9%
Ni2+
-
2 mM Ni2+ decreases CM0819 activity by 41.8%
prephenate
-
competitive
prephenate
-
competitive inhibition
tyrosine
is a negative effector for the enzyme; is a negative effector for the enzyme
tyrosine
inhibits about 20fold
tyrosine
Q9Y7B2
0.05 mM, heterotrophic feedback-inhibitor
tyrosine
heterotrophic feedback inhibitor
tyrosine
is a negative effector for the enzyme; is a negative effector for the enzyme
tyrosine
heterotrophic feedback inhibitor
tyrosine
competitive inhibition, 0.5 M tyrosine leads to 40% inhibition
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
-
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
activity is not affected by both amino acids Phe and Tyr at concentrations up to 0.5 mM
-
additional information
-
activity is not affected by both amino acids Phe and Tyr at concentrations up to 0.5 mM
-
additional information
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins; the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins; the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
-
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins; the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
-
the enzyme is greatly inhibited at acidic pH. L-phenylalanine, L-tyrosine, and L-tryptophan moderately enhance activity at low concentrations, but they inhibit the enzyme at higher concentrations
-
additional information
-
Unlike the other known prokaryotic CMs, the Mycobacterium tuberculosis enzyme exhibits allosteric regulation by aromatic amino acids, a feature limited to the eukaryotic CMs. The active site of MtbCM is seen to be blocked due to the presence of a sulfate ion in the structure. It therefore appears that sulphate acts as an inhibitor of the enzyme by blocking the entry of the substrate into the active site. In MtbCM the allosteric site is close to the active site
-
additional information
aza inhibitors. Competitive inhibition, Saccharomyces cerevisiae chorismate mutase inhibitors and the substrate chorismic acid used for pharmacophore model generation. These inhibitors do not alter Vmax at the higher concentration of substrate (1-5 mM)
-
additional information
-
aza inhibitors. Competitive inhibition, Saccharomyces cerevisiae chorismate mutase inhibitors and the substrate chorismic acid used for pharmacophore model generation. These inhibitors do not alter Vmax at the higher concentration of substrate (1-5 mM)
-
additional information
*MtCM is not regulated by the aromatic amino acids. The x-ray structure of *MtCM does not have an allosteric regulatory site in the protein
-
additional information
-
*MtCM is not regulated by the aromatic amino acids. The x-ray structure of *MtCM does not have an allosteric regulatory site in the protein
-
additional information
development and synthesis of transition state analogues and small molecule compounds as enzyme inhibitors
-
additional information
-
development and synthesis of transition state analogues and small molecule compounds as enzyme inhibitors
-
additional information
-
discovery and structure optimization of a series of isatin derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors, synthesis of enzyme inhibitors, overview
-
additional information
identification and structure-activity relationship study of carvacrol derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors, structure-based e-pharmacophore modeling, overview. Database screening using the crystal structure of the MTB CM bound transition state intermediate (PDB ID 2FP2) as framework. No inhibition by 3-(6-(benzyloxy)-1H-indol-1-yl)propanoic acid, 5-isopropyl-2-methylphenyl acetate, 4-bromo-5-isopropyl-2-methylphenol, 4-nitro-5-isopropyl-2-methylphenol, 4-isopropyl-2-methoxy-1-methylbenzene, 4-bromo-2-isopropyl-5-methylphenol, 4-nitro-2-isopropyl-5-methylphenol, and 4-chloro-2-isopropyl-5-methylphenol
-
additional information
-
identification and structure-activity relationship study of carvacrol derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors, structure-based e-pharmacophore modeling, overview. Database screening using the crystal structure of the MTB CM bound transition state intermediate (PDB ID 2FP2) as framework. No inhibition by 3-(6-(benzyloxy)-1H-indol-1-yl)propanoic acid, 5-isopropyl-2-methylphenyl acetate, 4-bromo-5-isopropyl-2-methylphenol, 4-nitro-5-isopropyl-2-methylphenol, 4-isopropyl-2-methoxy-1-methylbenzene, 4-bromo-2-isopropyl-5-methylphenol, 4-nitro-2-isopropyl-5-methylphenol, and 4-chloro-2-isopropyl-5-methylphenol
-
additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
-