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(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
?
L-2-amino-6-oxopimelate + L-glutamate + H2O
LL-2,6-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
LL-2,6-diaminopimelate + 2-oxoglutarate
2,3,4,5-tetrahydrodipicolinate + L-glutamate + H2O
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
meso-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
additional information
?
-
L-2-amino-6-oxopimelate + L-glutamate + H2O
LL-2,6-diaminopimelate + 2-oxoglutarate
-
-
-
-
?
L-2-amino-6-oxopimelate + L-glutamate + H2O
LL-2,6-diaminopimelate + 2-oxoglutarate
-
-
-
r
L-2-amino-6-oxopimelate + L-glutamate + H2O
LL-2,6-diaminopimelate + 2-oxoglutarate
-
-
-
-
r
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
-
slightly active (1%-2%) with meso-diaminopimelate, lysine and L-ornithine
-
-
r
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
-
-
-
-
r
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
-
-
-
-
r
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
no activity observed with pyruvate, prephenate, oxaloacetate and oxovalerate
-
-
r
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
-
-
-
-
r
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
no activity observed with pyruvate, prephenate, oxaloacetate and oxovalerate
-
-
r
L-glutamate + tetrahydrodipicolinate + H2O
LL-diaminopimelate + 2-oxoglutarate
-
-
-
-
r
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
-
-
r
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
-
-
r
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
WP_009961032
-
-
-
?
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
-
-
r
LL-2,6-diaminoheptanedioate + 2-oxoglutarate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
-
-
-
-
r
LL-2,6-diaminopimelate + 2-oxoglutarate
2,3,4,5-tetrahydrodipicolinate + L-glutamate + H2O
-
slightly active (1%-8%) with meso-diaminopimelate, L-lysine, L-ornithine, pyruvate, oxaloacetate and oxovalerate
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
2,3,4,5-tetrahydrodipicolinate + L-glutamate + H2O
-
slightly active (1%-8%) with meso-diaminopimelate, L-lysine, L-ornithine, pyruvate, oxaloacetate and oxovalerate
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
r
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-2,6-diaminopimelate + 2-oxoglutarate
L-2-amino-6-oxopimelate + L-glutamate + H2O
-
-
-
?
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
-
-
-
r
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
-
-
?
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
also active (17%-21%) with lysine, L-ornithine and cystathionine
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-
r
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
-
-
-
r
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
no activity observed with meso-diaminopimelate, L-lysine and L-ornithine
-
-
r
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
-
-
-
r
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
no activity observed with meso-diaminopimelate, L-lysine and L-ornithine
-
-
r
LL-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
-
-
-
r
meso-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
-
-
-
r
meso-diaminopimelate + 2-oxoglutarate
L-glutamate + tetrahydrodipicolinate + H2O
-
-
-
?
additional information
?
-
-
no substrate: m-diaminopimelate, lysine, ornithine, no amino acceptor: oxaloacetate, pyruvate
-
-
?
additional information
?
-
no substrate: m-diaminopimelate, lysine, ornithine, no amino acceptor: oxaloacetate, pyruvate
-
-
?
additional information
?
-
enzyme in the biosynthesis of L-lysine
-
-
?
additional information
?
-
-
enzyme in the biosynthesis of L-lysine
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-
?
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(2-[(E)-[1-(4-chlorophenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
-
14% inhibition at 0.01 mM
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
(2-[(E)-[1-methyl-3-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
-
17% inhibition at 0.01 mM
(2E)-2-cyano-3-[5-(dimethylamino)furan-2-yl]-N-(3,4-dimethylphenyl)prop-2-enamide
-
14% inhibition at 0.01 mM
(2Z)-N'-nitro-2-[[5-(3-nitrophenyl)furan-2-yl]methylidene]hydrazinecarboximidamide
-
13% inhibition at 0.01 mM
(3E)-1-[(4-methoxyphenyl)sulfonyl]-3-[4-oxo-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
-
18% inhibition at 0.01 mM
(3E)-1-[(4-methylphenyl)sulfonyl]-3-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)-1,3-dihydro-2H-indol-2-one
-
25% inhibition at 0.01 mM
(3E)-3-[2-(2,4-dimethyl-1,3-thiazol-5-yl)-2-oxoethylidene]-3,4-dihydroquinoxalin-2(1H)-one
-
18% inhibition at 0.01 mM
(3E)-3-[2-oxo-2-(thiophen-2-yl)ethylidene]-3,4-dihydroquinoxalin-2(1H)-one
-
15% inhibition at 0.01 mM
(3Z)-3-(2,4-dimethoxybenzylidene)-5-phenylfuran-2(3H)-one
-
14% inhibition at 0.01 mM
(5E)-5-(1H-indol-2-ylmethylidene)-1-(4-methylphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
16% inhibition at 0.01 mM
(5E)-5-[(1-benzyl-1H-indol-2-yl)methylidene]-1-(2-methoxyphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
20% inhibition at 0.01 mM
(5E)-5-[(1-methyl-1H-indol-2-yl)methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
35% inhibition at 0.01 mM
(5E)-5-[(1-methyl-1H-indol-2-yl)methylidene]-1-prop-2-en-1-yl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
45% inhibition at 0.01 mM
(5E)-5-[[1-(4-nitrobenzyl)-1H-indol-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
33% inhibition at 0.01 mM
(5Z)-1-(3-bromophenyl)-5-(furan-2-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
17% inhibition at 0.01 mM
(5Z)-3-(1,1-dioxidotetrahydrothiophen-3-yl)-5-[[1-phenyl-3-(thiophen-2-yl)-1H-pyrazol-4-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
13% inhibition at 0.01 mM
(5Z)-5-(3-iodo-4-methoxybenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
29% inhibition at 0.01 mM
(5Z)-5-[(3-methylthiophen-2-yl)methylidene]-3-(1-phenylethyl)-2-thioxo-1,3-thiazolidin-4-one
-
13% inhibition at 0.01 mM
(5Z)-5-[(3-methylthiophen-2-yl)methylidene]-3-(tetrahydrofuran-2-ylmethyl)-2-thioxo-1,3-thiazolidin-4-one
-
14% inhibition at 0.01 mM
(5Z)-5-[(6-bromo-1,3-benzodioxol-5-yl)methylidene]-2-(4-methylphenyl)-1,3-thiazol-4(5H)-one
-
13% inhibition at 0.01 mM
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
(5Z)-5-[[5-(2-bromo-4-nitrophenyl)furan-2-yl]methylidene]-2-imino-1,3-thiazolidin-4-one
-
13% inhibition at 0.01 mM
(5Z)-5-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-1-(4-methoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
20% inhibition at 0.01 mM
(Z)-3-amino-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
-
-
(Z)-3-ethyl-5-(2-hydroxybenzylidene)-2-thioxothiazolidin-4-one
-
-
(Z)-3-ethyl-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
-
-
(Z)-3-ethyl-5-(naphthalen-1-ylmethylene)-2-thioxothiazolidin-4-one
-
-
(Z)-3-ethyl-5-(quinolin-5-ylmethylene)-2-thioxothiazolidin-4-one
-
-
(Z)-5-(2-hydroxybenzylidene)-2-thioxothiazolidin-4-one
-
-
(Z)-5-(4-(dimethylamino)benzylidene)-2-thioxothiazolidin-4-one
-
-
(Z)-5-(4-chlorobenzylidene)-2-thioxothiazolidin-4-one
-
-
(Z)-5-(4-chlorobenzylidene)-3-ethyl-2-thioxothiazolidin-4-one
-
-
(Z)-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
-
-
(Z)-5-benzylidene-3-ethyl-2-thioxothiazolidin-4-one
-
-
(Z)-N -(5-((5-(4-nitrophenyl)furan-2-yl)methylene)-4-oxo-2-thioxothiazolidin-3-yl)acetamide
-
-
(Z)-N-(5-(4-methoxybenzylidene)-4-oxo-2-thioxothiazolidin-3-yl)acetamide
-
-
1,3-bis((7-chloro-4-quinolinyl)amino)-2-propanol
-
NSC_5485, potential drug candidate that can inhibit the enzymatic activity of enzyme CtDAP-AT
1,3-dimethyl-5-[[1-(3-nitrophenyl)-1H-pyrrol-2-yl]methylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
13% inhibition at 0.01 mM
1-(4-fluorophenyl)-2-[[4-phenyl-5-(3,4,5-trimethoxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]ethanone
-
14% inhibition at 0.01 mM
2-(2-[(E)-[1-(4-fluorophenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-phenylacetamide
-
18% inhibition at 0.01 mM
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
2-[(2E)-2-(2-oxo-5-phenylfuran-3(2H)-ylidene)hydrazinyl]benzoic acid
-
16% inhibition at 0.01 mM
2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide
3-cyclopropyl-N'-[(1E)-1-(4-methylphenyl)ethylidene]-1H-pyrazole-5-carbohydrazide
-
14% inhibition at 0.01 mM
3-[2-[(4-acetylphenyl)amino]-1,3-thiazol-4-yl]-2H-chromen-2-one
-
16% inhibition at 0.01 mM
4-chloro-N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
-
-
4-fluoro-N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
-
-
4-[(E)-[2-(2-chlorophenyl)-5-oxo-1,3-oxazol-4(5H)-ylidene]methyl]-2-hydroxyphenyl 2-chlorobenzoate
-
30% inhibition at 0.01 mM
5-(4-methylphenyl)-4-[[(E)-(2,4,5-trimethoxyphenyl)methylidene]amino]-4H-1,2,4-triazole-3-thiol
-
18% inhibition at 0.01 mM
5-([1-[2-(3,4-dimethylphenoxy)ethyl]-1H-indol-2-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
-
28% inhibition at 0.01 mM
5-[(5-hydroxy-1-phenyl-1H-pyrazol-4-yl)methylidene]-1,3-dimethylpyrimidine-2,4,6(1H,3H,5H)-trione
-
20% inhibition at 0.01 mM
5-[3-[(2-chlorobenzyl)oxy]-4-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
48% inhibition at 0.01 mM
8-methoxy-3-[(2-methylprop-2-en-1-yl)oxy]-6H-benzo[c]chromen-6-one
-
25% inhibition at 0.01 mM
Barbiturate
binding structure model
ethyl (5Z)-5-[[4-(dimethylamino)phenyl]methylidene]-2-[(4-methoxyphenyl)amino]-4-oxo-4,5-dihydrothiophene-3-carboxylate
-
22% inhibition at 0.01 mM
ethyl (5Z)-5-[[4-(dimethylamino)phenyl]methylidene]-2-[(4-nitrophenyl)amino]-4-oxo-4,5-dihydrothiophene-3-carboxylate
-
19% inhibition at 0.01 mM
ethyl 4-(5-[(Z)-[2,4,6-trioxo-1-(prop-2-en-1-yl)tetrahydropyrimidin-5(2H)-ylidene]methyl]furan-2-yl)benzoate
-
16% inhibition at 0.01 mM
hydrazide
binding structure model
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-5-nitro-3-phenyl-1H-indole-2-carbohydrazide
-
15% inhibition at 0.01 mM
N'-[(Z)-(4-fluorophenyl)methylidene]-3-(naphthalen-2-yl)-1H-pyrazole-5-carbohydrazide
-
14% inhibition at 0.01 mM
N-[(2E,5Z)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-4-oxo-1,3-thiazolidin-2-ylidene]acetamide
-
52% inhibition at 0.01 mM
N-[(5E)-5-[(5-bromofuran-2-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetamide
-
13% inhibition at 0.01 mM
N-[(5Z)-5-[(5-bromofuran-2-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetamide
-
-
N-[2-(hydrazinylcarbonyl)-4,5-dimethoxyphenyl]benzenesulfonamide
-
-
N-[2-(hydrazinylcarbonyl)-5-(trifluoromethyl)phenyl]benzenesulfonamide
-
-
N-[2-(hydrazinylcarbonyl)-5-methoxyphenyl]benzenesulfonamide
-
-
N-[2-(hydrazinylcarbonyl)-5-methylphenyl]benzenesulfonamide
-
-
N-[2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
-
-
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
N-[3-[(2,5-dimethoxyphenyl)amino]quinoxalin-2-yl]-3-nitrobenzenesulfonamide
-
13% inhibition at 0.01 mM
N-[4,5-difluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
-
-
N-[5-chloro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
-
-
N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]-4-methoxybenzenesulfonamide
-
-
N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]-4-methylbenzenesulfonamide
-
-
N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
-
-
N-[[2-(2-chlorophenyl)-1,3-benzoxazol-5-yl]carbamothioyl]-3-methyl-1-benzofuran-2-carboxamide
-
19% inhibition at 0.01 mM
rhodanine
binding structure model
thiobarbiturate
binding structure model
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
-
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
-
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
WP_009961032
-
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
13% inhibition at 0.01 mM
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
WP_009961032
-
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
-
15% inhibition at 0.01 mM
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
-
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
-
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
WP_009961032
-
2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide
-
2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide
-
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
-
33% inhibition at 0.01 mM
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
-
-
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
-
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
-
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
WP_009961032
-
additional information
-
not inhibitory: m-diaminopimelate, lysine, ornithine
-
additional information
not inhibitory: m-diaminopimelate, lysine, ornithine
-
additional information
-
not inhibited by (Z)-5-benzylidene-2-thioxothiazolidin-4-one, (Z)-5-(naphthalen-1-ylmethylene)-2-thioxothiazolidin-4-one, (Z)-3-amino-5-benzylidene-2-thioxothiazolidin-4-one, (Z)-3-amino-5-(4-chlorobenzylidene)-2-thioxothiazolidin-4-one, (Z)-N-(5-benzylidene-4-oxo-2-thioxothiazolidin-3-yl)-acetamide, (Z)-N-(5-(4-chlorobenzylidene)-4-oxo-2-thioxothiazolidin-3-yl)acetamide, and (Z)-5-(2-nitrobenzylidene)-2-thioxothiazolidin-4-one
-
additional information
-
high-throughput virtual screening for potential enzyme inhibitors using the optimized and corrected PLP-bound L,Ldiaminopimelate aminotransferase structure based on the crystal structure, PDB ID 3ASB. Comparative molecular dynamics simulation studies of enzyme CtDAP-AT in apoform and in complex with potential inhibitors, intermolecular interaction profiling of the compounds in complex with CtDAP-AT
-
additional information
comprehensive inhibition study comparing the kinetic activity of DapL orthologs using small molecule inhibitors and recombinant enzymes from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii. Enzyme active sites are conserved, although the second shell of residues close to the active site are not. The enzymes respond differently to the inhibitors
-
additional information
-
comprehensive inhibition study comparing the kinetic activity of DapL orthologs using small molecule inhibitors and recombinant enzymes from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii. Enzyme active sites are conserved, although the second shell of residues close to the active site are not. The enzymes respond differently to the inhibitors
-
additional information
comprehensive inhibition study comparing the kinetic activity of DapL orthologs using small molecule inhibitors and recombinant enzymes from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii. Enzyme active sites are conserved, although the second shell of residues close to the active site are not. the enzymes respond differntly to the inhibors
-
additional information
-
comprehensive inhibition study comparing the kinetic activity of DapL orthologs using small molecule inhibitors and recombinant enzymes from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii. Enzyme active sites are conserved, although the second shell of residues close to the active site are not. the enzymes respond differntly to the inhibors
-
additional information
WP_009961032
comprehensive inhibition study comparing the kinetic activity of DapL orthologs using small molecule inhibitors and recombinant enzymes from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii. Enzyme active sites are conserved, although the second shell of residues close to the active site are not. The enzymes respond differently to the inhibitors. 2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide is not inhibitory with Verrucomicrobium spinosum DapL
-
additional information
-
comprehensive inhibition study comparing the kinetic activity of DapL orthologs using small molecule inhibitors and recombinant enzymes from Leptospira interrogans, Verrucomicrobium spinosum and Chlamydomonas reinhardtii. Enzyme active sites are conserved, although the second shell of residues close to the active site are not. The enzymes respond differently to the inhibitors. 2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide is not inhibitory with Verrucomicrobium spinosum DapL
-
additional information
rhodanine, barbiturate, hydrazide, and thiobarbiturate associations with VsDapL are supported by molecular dynamics simulations, docking study, overview
-
additional information
-
rhodanine, barbiturate, hydrazide, and thiobarbiturate associations with VsDapL are supported by molecular dynamics simulations, docking study, overview
-
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0.065
(2-[(E)-[1-(4-chlorophenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
Arabidopsis thaliana
-
-
0.037 - 0.048
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
0.037
(2-[(E)-[1-methyl-3-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
Arabidopsis thaliana
-
-
0.2
(2E)-2-cyano-3-[5-(dimethylamino)furan-2-yl]-N-(3,4-dimethylphenyl)prop-2-enamide
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.2
(2Z)-N'-nitro-2-[[5-(3-nitrophenyl)furan-2-yl]methylidene]hydrazinecarboximidamide
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.194
(3E)-1-[(4-methoxyphenyl)sulfonyl]-3-[4-oxo-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
Arabidopsis thaliana
-
-
0.07
(3E)-1-[(4-methylphenyl)sulfonyl]-3-(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)-1,3-dihydro-2H-indol-2-one
Arabidopsis thaliana
-
-
0.056
(3E)-3-[2-(2,4-dimethyl-1,3-thiazol-5-yl)-2-oxoethylidene]-3,4-dihydroquinoxalin-2(1H)-one
Arabidopsis thaliana
-
-
0.031
(3E)-3-[2-oxo-2-(thiophen-2-yl)ethylidene]-3,4-dihydroquinoxalin-2(1H)-one
Arabidopsis thaliana
-
-
0.159
(3Z)-3-(2,4-dimethoxybenzylidene)-5-phenylfuran-2(3H)-one
Arabidopsis thaliana
-
-
0.164
(5E)-5-(1H-indol-2-ylmethylidene)-1-(4-methylphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.062
(5E)-5-[(1-benzyl-1H-indol-2-yl)methylidene]-1-(2-methoxyphenyl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.075
(5E)-5-[(1-methyl-1H-indol-2-yl)methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.033
(5E)-5-[(1-methyl-1H-indol-2-yl)methylidene]-1-prop-2-en-1-yl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.069
(5E)-5-[[1-(4-nitrobenzyl)-1H-indol-2-yl]methylidene]-1-(prop-2-en-1-yl)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.2
(5Z)-1-(3-bromophenyl)-5-(furan-2-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.117
(5Z)-3-(1,1-dioxidotetrahydrothiophen-3-yl)-5-[[1-phenyl-3-(thiophen-2-yl)-1H-pyrazol-4-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Arabidopsis thaliana
-
-
0.18
(5Z)-5-(3-iodo-4-methoxybenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Arabidopsis thaliana
-
-
0.127
(5Z)-5-[(3-methylthiophen-2-yl)methylidene]-3-(1-phenylethyl)-2-thioxo-1,3-thiazolidin-4-one
Arabidopsis thaliana
-
-
0.2
(5Z)-5-[(3-methylthiophen-2-yl)methylidene]-3-(tetrahydrofuran-2-ylmethyl)-2-thioxo-1,3-thiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.13
(5Z)-5-[(6-bromo-1,3-benzodioxol-5-yl)methylidene]-2-(4-methylphenyl)-1,3-thiazol-4(5H)-one
Arabidopsis thaliana
-
-
0.046 - 0.25
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
0.085
(5Z)-5-[[5-(2-bromo-4-nitrophenyl)furan-2-yl]methylidene]-2-imino-1,3-thiazolidin-4-one
Arabidopsis thaliana
-
-
0.042
(5Z)-5-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-1-(4-methoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
Arabidopsis thaliana
-
-
0.155
(Z)-3-amino-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-3-ethyl-5-(2-hydroxybenzylidene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM, in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-3-ethyl-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM, in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-3-ethyl-5-(naphthalen-1-ylmethylene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM,in 100 mM HEPES-KOH, pH 7.6
0.19
(Z)-3-ethyl-5-(quinolin-5-ylmethylene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-5-(2-hydroxybenzylidene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM, in 100 mM HEPES-KOH, pH 7.6
0.127
(Z)-5-(4-(dimethylamino)benzylidene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-5-(4-chlorobenzylidene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM, in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-5-(4-chlorobenzylidene)-3-ethyl-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM, in 100 mM HEPES-KOH, pH 7.6
0.142
(Z)-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-5-benzylidene-3-ethyl-2-thioxothiazolidin-4-one
Arabidopsis thaliana
-
IC50 above 0.2 mM, in 100 mM HEPES-KOH, pH 7.6
0.073
(Z)-N -(5-((5-(4-nitrophenyl)furan-2-yl)methylene)-4-oxo-2-thioxothiazolidin-3-yl)acetamide
Arabidopsis thaliana
-
in 100 mM HEPES-KOH, pH 7.6
0.2
(Z)-N-(5-(4-methoxybenzylidene)-4-oxo-2-thioxothiazolidin-3-yl)acetamide
Arabidopsis thaliana
-
IC50 above 0.2 mM, in 100 mM HEPES-KOH, pH 7.6
0.2
1,3-dimethyl-5-[[1-(3-nitrophenyl)-1H-pyrrol-2-yl]methylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.2
1-(4-fluorophenyl)-2-[[4-phenyl-5-(3,4,5-trimethoxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]ethanone
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.052
2-(2-[(E)-[1-(4-fluorophenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-phenylacetamide
Arabidopsis thaliana
-
-
0.025 - 0.057
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
0.039
2-[(2E)-2-(2-oxo-5-phenylfuran-3(2H)-ylidene)hydrazinyl]benzoic acid
Arabidopsis thaliana
-
-
0.025 - 0.033
2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide
0.2
3-cyclopropyl-N'-[(1E)-1-(4-methylphenyl)ethylidene]-1H-pyrazole-5-carbohydrazide
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.2
3-[2-[(4-acetylphenyl)amino]-1,3-thiazol-4-yl]-2H-chromen-2-one
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.0053
4-chloro-N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0075
4-fluoro-N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.081
4-[(E)-[2-(2-chlorophenyl)-5-oxo-1,3-oxazol-4(5H)-ylidene]methyl]-2-hydroxyphenyl 2-chlorobenzoate
Arabidopsis thaliana
-
-
0.2
5-(4-methylphenyl)-4-[[(E)-(2,4,5-trimethoxyphenyl)methylidene]amino]-4H-1,2,4-triazole-3-thiol
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.099
5-([1-[2-(3,4-dimethylphenoxy)ethyl]-1H-indol-2-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
Arabidopsis thaliana
-
-
0.045
5-[(5-hydroxy-1-phenyl-1H-pyrazol-4-yl)methylidene]-1,3-dimethylpyrimidine-2,4,6(1H,3H,5H)-trione
Arabidopsis thaliana
-
-
0.121
5-[3-[(2-chlorobenzyl)oxy]-4-methoxybenzylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.2
8-methoxy-3-[(2-methylprop-2-en-1-yl)oxy]-6H-benzo[c]chromen-6-one
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.2
ethyl (5Z)-5-[[4-(dimethylamino)phenyl]methylidene]-2-[(4-methoxyphenyl)amino]-4-oxo-4,5-dihydrothiophene-3-carboxylate
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.141
ethyl (5Z)-5-[[4-(dimethylamino)phenyl]methylidene]-2-[(4-nitrophenyl)amino]-4-oxo-4,5-dihydrothiophene-3-carboxylate
Arabidopsis thaliana
-
-
0.2
ethyl 4-(5-[(Z)-[2,4,6-trioxo-1-(prop-2-en-1-yl)tetrahydropyrimidin-5(2H)-ylidene]methyl]furan-2-yl)benzoate
Arabidopsis thaliana
-
IC50 above 0.2 mM
0.045
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-5-nitro-3-phenyl-1H-indole-2-carbohydrazide
Arabidopsis thaliana
-
-
0.161
N'-[(Z)-(4-fluorophenyl)methylidene]-3-(naphthalen-2-yl)-1H-pyrazole-5-carbohydrazide
Arabidopsis thaliana
-
-
0.078
N-[(2E,5Z)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-4-oxo-1,3-thiazolidin-2-ylidene]acetamide
Arabidopsis thaliana
-
-
0.041
N-[(5E)-5-[(5-bromofuran-2-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetamide
Arabidopsis thaliana
-
-
0.041
N-[(5Z)-5-[(5-bromofuran-2-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0207
N-[2-(hydrazinylcarbonyl)-4,5-dimethoxyphenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0038
N-[2-(hydrazinylcarbonyl)-5-(trifluoromethyl)phenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0045
N-[2-(hydrazinylcarbonyl)-5-methoxyphenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0079
N-[2-(hydrazinylcarbonyl)-5-methylphenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0132
N-[2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.005 - 0.047
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
0.153
N-[3-[(2,5-dimethoxyphenyl)amino]quinoxalin-2-yl]-3-nitrobenzenesulfonamide
Arabidopsis thaliana
-
-
0.0059
N-[4,5-difluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0041
N-[5-chloro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0034
N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]-4-methoxybenzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0056
N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]-4-methylbenzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.0025
N-[5-fluoro-2-(hydrazinylcarbonyl)phenyl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.083
N-[[2-(2-chlorophenyl)-1,3-benzoxazol-5-yl]carbamothioyl]-3-methyl-1-benzofuran-2-carboxamide
Arabidopsis thaliana
-
-
0.037
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
Chlamydomonas reinhardtii
pH 7.6, temperature not specified in the publication
0.047
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
Verrucomicrobium spinosum
WP_009961032
pH 7.6, temperature not specified in the publication
0.048
(2-[(E)-[1-(4-methylphenyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetic acid
Leptospira interrogans
pH 7.6, temperature not specified in the publication
0.046
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Arabidopsis thaliana
-
-
0.046
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Chlamydomonas reinhardtii
pH 7.6, temperature not specified in the publication
0.048
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Leptospira interrogans
pH 7.6, temperature not specified in the publication
0.25
(5Z)-5-[5-(2-chlorobenzyl)-2-hydroxybenzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Verrucomicrobium spinosum
WP_009961032
pH 7.6, temperature not specified in the publication
0.025
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
Arabidopsis thaliana
-
-
0.025
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
Chlamydomonas reinhardtii
pH 7.6, temperature not specified in the publication
0.028
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
Leptospira interrogans
pH 7.6, temperature not specified in the publication
0.057
2-thioxo-5-[(1,2,5-trimethyl-1H-pyrrol-3-yl)methylidene]dihydropyrimidine-4,6(1H,5H)-dione
Verrucomicrobium spinosum
WP_009961032
pH 7.6, temperature not specified in the publication
0.025
2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide
Leptospira interrogans
pH 7.6, temperature not specified in the publication
0.033
2-[2-[(E)-(4,6-dioxo-1-phenyl-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]-1H-indol-1-yl]-N-phenylacetamide
Chlamydomonas reinhardtii
pH 7.6, temperature not specified in the publication
0.005
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
Arabidopsis thaliana
-
-
0.005
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
Arabidopsis thaliana
-
pH not specified in the publication, temperature not specified in the publication
0.005
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
Chlamydomonas reinhardtii
pH 7.6, temperature not specified in the publication
0.0068
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
Leptospira interrogans
pH 7.6, temperature not specified in the publication
0.047
N-[3-(hydrazinylcarbonyl)naphthalen-2-yl]benzenesulfonamide
Verrucomicrobium spinosum
WP_009961032
pH 7.6, temperature not specified in the publication
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malfunction
Arabidopsis thaliana DAP mutant dapat shows reduced activity of the Lys biosynthesis enzyme L,L-diaminopimelate aminotransferase, physiological and metabolic impacts of impaired Lys biosynthesis, the mutation leads to metabolic shifts and growth inhibition, phenotype, overview. No differences in dark respiration between genotypes are observed, but a lower storage and consumption of starch and sugars is observed in dapat plants, also higher protein turnover but no differences in total amino acids during a diurnal cycle in dapat plants. Biochemical alterations rather than stomatal limitations are responsible for the decreased photosynthesis and growth of the dapat mutant, which mimics stress conditions associated with impairments in the Lys biosynthesis pathway
malfunction
-
Arabidopsis thaliana DAP mutant dapat shows reduced activity of the Lys biosynthesis enzyme L,L-diaminopimelate aminotransferase, physiological and metabolic impacts of impaired Lys biosynthesis, the mutation leads to metabolic shifts and growth inhibition, phenotype, overview. No differences in dark respiration between genotypes are observed, but a lower storage and consumption of starch and sugars is observed in dapat plants, also higher protein turnover but no differences in total amino acids during a diurnal cycle in dapat plants. Biochemical alterations rather than stomatal limitations are responsible for the decreased photosynthesis and growth of the dapat mutant, which mimics stress conditions associated with impairments in the Lys biosynthesis pathway
-
metabolism
the enzyme is involved in the lysine pathway, overview. Lysine is synthetized in the chloroplast using aspartate as a precursor. Dihydrodipicolinate synthase (DHDPS) is the first enzyme of lysine biosynthesis and it requires pyruvate export from the cytosol to the chloroplast. Under stress conditions, lysine is exported from the chloroplast to mitochondria to be degraded, and electrons are used as a donor for ATP synthesis
metabolism
the LL-diaminopimelate aminotransferase (DapL) pathway is a variant of the lysine biosynthetic pathway, overview
metabolism
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the enzyme is involved in the lysine pathway, overview. Lysine is synthetized in the chloroplast using aspartate as a precursor. Dihydrodipicolinate synthase (DHDPS) is the first enzyme of lysine biosynthesis and it requires pyruvate export from the cytosol to the chloroplast. Under stress conditions, lysine is exported from the chloroplast to mitochondria to be degraded, and electrons are used as a donor for ATP synthesis
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physiological function
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lysine biosynthesis pathway
physiological function
DapL is a homodimer that catalyzes the conversion of tetrahydrodipicolinate to LL-diaminopimelate in a single transamination reaction. The penultimate and ultimate products of the lysine biosynthesis pathway, meso-diaminopimelate and lysine, are key components of the Gram-negative and Gram-positive bacterial peptidoglycan cell wall
physiological function
the Verrucomicrobium spinosum dapL gene encodes a putative diaminopimelate aminotransferase, the gene expression rescues an Escherichia coli strain that is auxotrophic for meso-diaminopimelate. LL-Diaminopimelate aminotransferase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the transamination of L-tetrahydrodipicolinate to form LL-diaminopimelate. The reaction proceeds via a bimolecular ping-pong mechanism. First, the amino group from the donor molecule L-glutamate forms a covalent Schiff base with the PLP molecule tethered in the enzyme active site. This is followed by the transfer of the amino group to the acceptor molecule, L-tetrahydrodipicolinate, forming LL-diaminopimelate. Subsequent enzymes catalyze the epimerization to form meso-diaminopimelate and decarboxylation to yield L-lysine
additional information
comparative molecular dynamics simulations, ligand docking study, sequence comaprisons and three-dimensional homology modelling, active site structure, detailed overview. Key conserved active site residues are identified as I43, G44, Y74, E77, K111, Y134, N189, K251, N294, and R390
additional information
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comparative molecular dynamics simulations, ligand docking study, sequence comaprisons and three-dimensional homology modelling, active site structure, detailed overview. Key conserved active site residues are identified as I43, G44, Y74, E77, K111, Y134, N189, K251, N294, and R390
additional information
DapL enzyme structures comparisons
additional information
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DapL enzyme structures comparisons
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Hudson, A.O.; Singh, B.K.; Leustek, T.; Gilvarg, C.
An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants
Plant Physiol.
140
292-301
2006
Arabidopsis thaliana, Arabidopsis thaliana (Q93ZN9)
brenda
Watanabe, N.; Cherney, M.M.; van Belkum, M.J.; Marcus, S.L.; Flegel, M.D.; Clay, M.D.; Deyholos, M.K.; Vederas, J.C.; James, M.N.
Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and chlamydia
J. Mol. Biol.
371
685-702
2007
Arabidopsis thaliana (Q93ZN9), Arabidopsis thaliana
brenda
Hudson, A.O.; Gilvarg, C.; Leustek, T.
Biochemical and phylogenetic characterization of a novel diaminopimelate biosynthesis pathway in prokaryotes identifies a diverged form of LL-diaminopimelate aminotransferase
J. Bacteriol.
190
3256-3263
2008
Syntrophobacter fumaroxidans (A0LEA5), Methanothermobacter thermautotrophicus (O26158), Aquifex aeolicus (O66630), Chlamydia trachomatis (O84395), Desulfitobacterium hafniense (Q18T09), Methanosphaera stadtmanae (Q2NFU1), Moorella thermoacetica (Q2RK33), Trichormus variabilis (Q3MAL4), Trichormus variabilis (Q3MDN5), Synechocystis sp. (Q55828), Bacteroides fragilis (Q5LC03), Candidatus Protochlamydia amoebophila (Q6MDE0), Leptospira interrogans (Q72NJ3), Geobacter sulfurreducens (Q74GT3), Gloeobacter violaceus (Q7NDX4), Methanosarcina acetivorans (Q8TQ40)
brenda
Fan, C.; Clay, M.D.; Deyholos, M.K.; Vederas, J.C.
Exploration of inhibitors for diaminopimelate aminotransferase
Bioorg. Med. Chem.
18
2141-2151
2010
Arabidopsis thaliana
brenda
Watanabe, N.; Clay, M.D.; van Belkum, M.J.; Cherney, M.M.; Vederas, J.C.; James, M.N.
Mechanism of substrate recognition and PLP-induced conformational changes in LL-diaminopimelate aminotransferase from Arabidopsis thaliana
J. Mol. Biol.
384
1314-1329
2008
Arabidopsis thaliana (Q93ZN9), Arabidopsis thaliana
brenda
Hudson, A.O.; Giron, I.; Dobson, R.C.
Crystallization and preliminary X-ray diffraction analysis of L,L-diaminopimelate aminotransferase (DapL) from Chlamydomonas reinhardtii
Acta Crystallogr. Sect. F
67
140-143
2011
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC-1690
brenda
Sobolev, V.; Edelman, M.; Dym, O.; Unger, T.; Albeck, S.; Kirma, M.; Galili, G.
Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis
Acta Crystallogr. Sect. F
69
84-89
2013
Arabidopsis thaliana (Q9ZQI7), Arabidopsis thaliana
brenda
Watanabe, N.; James, M.N.
Structural insights for the substrate recognition mechanism of LL-diaminopimelate aminotransferase
Biochim. Biophys. Acta
1814
1528-1533
2011
Arabidopsis thaliana, Chlamydia trachomatis
brenda
Nachar, V.R.; Savka, F.C.; McGroty, S.E.; Donovan, K.A.; North, R.A.; Dobson, R.C.; Buckley, L.J.; Hudson, A.O.
Genomic and biochemical analysis of the diaminopimelate and lysine biosynthesis pathway in Verrucomicrobium spinosum: Identification and partial characterization of L,L-diaminopimelate aminotransferase and UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-meso-diaminopimelate ligase
Front. Microbiol.
3
183
2012
Verrucomicrobium spinosum, Verrucomicrobium spinosum DSM 4136T
brenda
Liu, Y.; White, R.H.; Whitman, W.B.
Methanococci use the diaminopimelate aminotransferase (DapL) pathway for lysine biosynthesis
J. Bacteriol.
192
3304-3310
2010
Methanococcus maripaludis
brenda
Watanabe, N.; Clay, M.D.; van Belkum, M.J.; Fan, C.; Vederas, J.C.; James, M.N.
The structure of LL-diaminopimelate aminotransferase from Chlamydia trachomatis: implications for its broad substrate specificity
J. Mol. Biol.
411
649-660
2011
Chlamydia trachomatis (O84395), Chlamydia trachomatis
brenda
Fan, C.; Vederas, J.C.
Synthesis and structure-activity relationships of o-sulfonamido-arylhydrazides as inhibitors of LL-diaminopimelate aminotransferase (LL-DAP-AT)
Org. Biomol. Chem.
10
5815-5819
2012
Arabidopsis thaliana
brenda
Dobson, R.C.; Giron, I.; Hudson, A.O.
L,L-diaminopimelate aminotransferase from Chlamydomonas reinhardtii: a target for algaecide development
PLoS ONE
6
e20439
2011
Chlamydomonas reinhardtii (A8IW39), Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CC-1690 (A8IW39)
brenda
McKinnie, S.M.; Rodriguez-Lopez, E.M.; Vederas, J.C.; Crowther, J.M.; Suzuki, H.; Dobson, R.C.; Leustek, T.; Triassi, A.J.; Wheatley, M.S.; Hudson, A.O.
Differential response of orthologous L,L-diaminopimelate aminotransferases (DapL) to enzyme inhibitory antibiotic lead compounds
Bioorg. Med. Chem.
22
523-530
2014
Chlamydomonas reinhardtii (A8IW39), Chlamydomonas reinhardtii, Leptospira interrogans (Q72NJ3), Leptospira interrogans, Verrucomicrobium spinosum (WP_009961032), Verrucomicrobium spinosum
brenda
Weatherhead, A.W.; Crowther, J.M.; Horne, C.R.; Meng, Y.; Coombes, D.; Currie, M.J.; Watkin, S.A.J.; Adams, L.E.; Parthasarathy, A.; Dobson, R.C.J.; Hudson, A.O.
Structure-function studies of the antibiotic target L,L-diaminopimelate aminotransferase from Verrucomicrobium spinosum reveal an unusual oligomeric structure
Biochemistry
59
2274-2288
2020
Verrucomicrobium spinosum (A0A6P3CW87), Verrucomicrobium spinosum
brenda
Adams, L.E.; Rynkiewicz, P.; Babbitt, G.A.; Mortensen, J.S.; North, R.A.; Dobson, R.C.J.; Hudson, A.O.
Comparative molecular dynamics simulations provide insight into antibiotic interactions a case study using the enzyme L,L-diaminopimelate aminotransferase (DapL)
Front. Mol. Biosci.
7
46
2020
Verrucomicrobium spinosum (A0A6P3CW87), Verrucomicrobium spinosum
brenda
Sadhasivam, A.; Vetrivel, U.
Identification of potential drugs targeting L,L-diaminopimelate aminotransferase of Chlamydia trachomatis an integrative pharmacoinformatics approach
J. Cell. Biochem.
120
2271-2288
2019
Chlamydia trachomatis
brenda
Cavalcanti, J.H.F.; Kirma, M.; Barros, J.A.S.; Quinhones, C.G.S.; Pereira-Lima, I.A.; Obata, T.; Nunes-Nesi, A.; Galili, G.; Fernie, A.R.; Avin-Wittenberg, T.; Araujo, W.L.
An L,L-diaminopimelate aminotransferase mutation leads to metabolic shifts and growth inhibition in Arabidopsis
J. Exp. Bot.
69
5489-5506
2018
Arabidopsis thaliana (Q93ZN9), Arabidopsis thaliana Col-0 (Q93ZN9)
brenda