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2'-deoxy-ATP + pantetheine 4'-phosphate
?
-
phosphorylation at 27% the rate of ATP
-
-
?
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
4'-phosphopantetheine + Mg2+-ATP
3'-dephospho-CoA + diphosphate
-
PPAT does not accept 4'-phosphopantothenoyl-Cys as a substrate
-
-
r
ATP + 4'-phosphopantetheine
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
diphosphate + 3'-dephospho-CoA
ATP + pantetheine 4'-phosphate
phosphopantetheine + Mg-ATP
dephospho-CoA + diphosphate
phosphopantetheine + MgATP2- + 4 H+
dephospho-CoA + diphosphate + Mg2+
-
coenzyme A (CoA) biosynthesis
-
-
?
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
-
important enzyme in CoA biosynthesis
-
-
r
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
-
coenzyme A biosynthetic pathway
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
no substrates are GTP, ITP, UTP, or CTP
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
involved in coenzyme A biosynthesis
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
no substrate is 4'-pantothenoyl-L-cysteine
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
diphosphate + 3'-dephospho-CoA
ATP + pantetheine 4'-phosphate
-
-
-
r
diphosphate + 3'-dephospho-CoA
ATP + pantetheine 4'-phosphate
-
-
-
r
diphosphate + 3'-dephospho-CoA
ATP + pantetheine 4'-phosphate
-
-
-
r
diphosphate + 3'-dephospho-CoA
ATP + pantetheine 4'-phosphate
-
-
-
r
phosphopantetheine + Mg-ATP
dephospho-CoA + diphosphate
-
-
-
-
r
phosphopantetheine + Mg-ATP
dephospho-CoA + diphosphate
-
essential hexameric enzyme that catalyzes the penultimate step in coenzyme A biosynthesis
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
phosphopantetheine + Mg-ATP
dephospho-CoA + diphosphate
-
essential hexameric enzyme that catalyzes the penultimate step in coenzyme A biosynthesis
-
-
r
phosphopantetheine + MgATP2- + 4 H+
dephospho-CoA + diphosphate + Mg2+
-
coenzyme A (CoA) biosynthesis
-
-
?
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
-
important enzyme in CoA biosynthesis
-
-
r
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
-
coenzyme A biosynthetic pathway
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
involved in coenzyme A biosynthesis
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
(2'R)-1-methyl-N4'-[3-(trifluoromethyl)phenyl]-1,2-dihydro-5'H-spiro[indole-3,2'-[1,3,5]triazine]-4',6'-diamine
identified by virtual screening. Compound directly binds and blocks access of substrates to the active site. The trifluoromethyl group of the ligand is oriented inside the protein molecule. One of the nitrogen atoms of the ligand forms contacts with Gly8 and Ser9. The NH2 interacts with the guanidine group of Arg90
(2S)-2-(3-chlorophenyl)-2-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]ethyl carbamate
-
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
(3R)-3-(3-chlorophenyl)-3-[(7-[[2-(3,5-dimethyl-1H-pyrazol-4-yl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
(3R)-3-([7-[(1-acetyl-2,3-dihydro-1H-indol-5-yl)amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl]amino)-3-(3-chlorophenyl)propanenitrile
1-[5-[(2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-7-yl)amino]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
2-(3,4-dihydroquinoline-1(2H)-carbonyl)-2,4-dihydro-5lambda6-[1,2,4]triazolo[5,1-c][1,2,4]benzothiadiazine-5,5(1H)-dione
identified by virtual screening. Compound directly binds and blocks access of substrates to the active site. The nitrogen and oxygen atoms of the sulfamide group of the inhibitor are involved in hydrogen bonding with Pro7 and form polar contacts with the residues Gly88 and Gly8. The nitrogen atom of the triazole ring interacts with the side group of His17
-
2-[(1S)-2-(4-chlorophenyl)cyclopentyl]-1H-benzimidazol-4-ol
-
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
2-[1-(4-chlorophenyl)pyrrolidin-2-yl]-1H-benzimidazol-4-ol
-
2-[2-(4-chlorophenyl)ethyl]-1H-benzimidazol-4-ol
-
2-[[(1R)-1-(3-chlorophenyl)-3-hydroxypropyl]amino]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
-
2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-ethyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
-
2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
-
2-[[(1S)-1-(3-chlorophenyl)-2-hydroxyethyl]amino]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
-
3'-dephospho coenzyme A
KD value 0.0032 mM
3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanamide
-
3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanoic acid
-
3-[(2S)-2-(4-hydroxy-1H-benzimidazol-2-yl)cyclopentyl]benzoic acid
-
3-[(4-fluorophenyl)methyl]-5-[1-[2-(trifluoromethyl)benzene-1-sulfonyl]piperidin-4-yl]-3H-[1,2,3]triazolo[4,5-d]pyrimidin-7-ol
identified by virtual screening. Compound directly binds and blocks access of substrates to the active site. The triazole and pyrimidine rings of the ligand form polar contacts with the side groups of Ser127, Ser128, and Arg90 and hydrogen bonds with the residues His17 and Val125
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
3-[4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-1-(methoxycarbonyl)piperidin-4-yl]propanoic acid
5-(4-hydroxy-1H-benzimidazol-2-yl)-1-methyl-6-phenylpiperidin-2-one
-
6-chloro-1-[(3-methylphenyl)methyl]-3-(morpholine-4-carbonyl)-4lambda6,1,2-benzothiadiazine-4,4(1H)-dione
identified by virtual screening. Compound directly binds and blocks access of substrates to the active site. One of the oxygen atoms of the sulfone group interacts with the main-chain nitrogen atoms of the residues Ser9 and Phe10. There are also polar contacts with His17 and Ser127
adenosine-5'-[(alpha,beta)-methyleno]triphosphate
-
D-amethopterin
a mixed-type inhibitor of HpPPAT activity, that simultaneously occupies the HpPPAT 4'-phosphopantetheine- and ATP-binding sites, the compound can serve as a lead compound in drug development, steady-state kinetic inhibition assay. Model of HpPPAT complexed with D-amethopterin, overview
deoxycholate
-
inactivation at 0.2%, activation at 0.01%
methyl (R)-4-(3-(2-cyano-1-((5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino)ethyl)benzyl)piperidine-1-carboxylate
methyl 4-(2-cyanoethyl)-4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]piperidine-1-carboxylate
methyl 4-(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]benzene-1-sulfonyl)piperidine-1-carboxylate
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-(3-hydroxypropyl)piperidine-1-carboxylate
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[(Z)-(methoxyimino)methyl]piperidine-1-carboxylate
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[[(2-hydroxyethyl)amino]methyl]piperidine-1-carboxylate
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)sulfanyl]piperidine-1-carboxylate
N-[(1R)-1-(3-chlorophenyl)ethyl]-5-methyl-1H-imidazo[4,5-b]pyridin-2-amine
-
-
N-[(1R)-1-(3-chlorophenyl)ethyl]-5-methyl[1,3]thiazolo[4,5-b]pyridin-2-amine
-
N2-[(1R)-1-(3-chlorophenyl)ethyl]-5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidine-2,7-diamine
-
pantetheine
-
potent inhibitor
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
-
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
-
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
-
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
-
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
lead compound as selective, small molecule inhibitor, displays modest cellular potency against the efflux-deficient Escherichia coli DeltatolC mutant strain
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
lead compound as selective, small molecule inhibitor
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
lead compound as selective, small molecule inhibitor, displays modest cellular potency against the efflux-deficient Escherichia coli DeltatolC mutant strain
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
lead compound as selective, small molecule inhibitor
(3R)-3-(3-chlorophenyl)-3-[(7-[[2-(3,5-dimethyl-1H-pyrazol-4-yl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
-
(3R)-3-(3-chlorophenyl)-3-[(7-[[2-(3,5-dimethyl-1H-pyrazol-4-yl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
-
(3R)-3-([7-[(1-acetyl-2,3-dihydro-1H-indol-5-yl)amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl]amino)-3-(3-chlorophenyl)propanenitrile
-
(3R)-3-([7-[(1-acetyl-2,3-dihydro-1H-indol-5-yl)amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl]amino)-3-(3-chlorophenyl)propanenitrile
-
1-[5-[(2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-7-yl)amino]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
1-[5-[(2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-7-yl)amino]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
-
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
slight inhibition in vivo
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
-
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
-
-
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
-
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
-
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
-
-
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
-
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
slight inhibition in vivo
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
-
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
-
3-[4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-1-(methoxycarbonyl)piperidin-4-yl]propanoic acid
-
3-[4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-1-(methoxycarbonyl)piperidin-4-yl]propanoic acid
-
acetyl-CoA
allosteric inhibitor
CoA
-
-
CoA
the enzyme is allosteric in nature and regulated by coenzyme A through feedback inhibition, PPAT forms a ternary complex with diphosphate and coenzyme A
coenzyme A
KD value 0.0012 mM
coenzyme A
feedback inhibition
methyl (R)-4-(3-(2-cyano-1-((5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino)ethyl)benzyl)piperidine-1-carboxylate
-
methyl (R)-4-(3-(2-cyano-1-((5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino)ethyl)benzyl)piperidine-1-carboxylate
-
methyl 4-(2-cyanoethyl)-4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]piperidine-1-carboxylate
-
methyl 4-(2-cyanoethyl)-4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]piperidine-1-carboxylate
-
methyl 4-(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]benzene-1-sulfonyl)piperidine-1-carboxylate
-
methyl 4-(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]benzene-1-sulfonyl)piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-(3-hydroxypropyl)piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-(3-hydroxypropyl)piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[(Z)-(methoxyimino)methyl]piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[(Z)-(methoxyimino)methyl]piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[[(2-hydroxyethyl)amino]methyl]piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[[(2-hydroxyethyl)amino]methyl]piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)sulfanyl]piperidine-1-carboxylate
-
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)sulfanyl]piperidine-1-carboxylate
-
PTX040334
-
IC50: 0.03 mM
PTX040334
-
no inhibition
PTX042695
-
IC50: 0.000006 mM
PTX042695
-
no inhibition
additional information
compound library screening, the series of reversible inhibitors show inhibition of cell growth of Gram-positive species but not of Candida albicans. MIC values, overview. Compounds HTS hit, A, B, C, and D show poor inhibition in vivo
-
additional information
-
compound library screening, the potency of the series is optimized using structure-based design, resulting in inhibition of cell growth of Gram-positive species. MIC values, overview
-
additional information
-
no inhibition is observed with AMPCPP, ATP-gamma-S, ADPPNP, or ADP at concentrations up to 1 mM and although no inhibition is observed with acetyl-CoA, desulfo-CoA, and palmitoyl-CoA at concentrations up to 500 mM
-
additional information
compound library screening, the potency of the series is optimized using structure-based design, resulting in inhibition of cell growth of Gram-positive species. Levels of inhibitory activity of compounds against Escherichia coli PPAT are measured in the reverse direction, MIC values, overview
-
additional information
3DQSAR and molecular dynamic simulations to reveal the structural determinants of inhibitors with scaffolds triazolopyrimidinone, triazolopyrimidine and azabenzimidazole
-
additional information
compound library screening, the potency of the series is optimized using structure-based design, resulting in inhibition of cell growth of Gram-positive species. Levels of inhibitory activity of compounds against Haemophilus influenzae PPAT are measured in the reverse direction, MIC values, overview
-
additional information
inhibitor virtual high-throughput screening using the HpPPAT crystal structure, docking study, overview
-
additional information
-
inhibitor virtual high-throughput screening using the HpPPAT crystal structure, docking study, overview
-
additional information
compound library screening, the series of reversible inhibitors show inhibition of cell growth of Gram-positive species but no or only slight inhibition of the human A-549 tumor cells, MIC values, overview. levels of inhibitory activity of compounds against Homo sapiens PPAT are measured in the forward direction. Only compound C shows poor inhibition in vivo
-
additional information
transition of PPAT in Pseudomonas aeruginosa from substrate binding to inhibitory states is triggered by an arginine switch
-
additional information
-
transition of PPAT in Pseudomonas aeruginosa from substrate binding to inhibitory states is triggered by an arginine switch
-
additional information
-
compound library screening, mode-of-inhibition studies with Staphylococcus aureus PPAT demonstrate representatives of this series to be reversible inhibitors competitive versus phosphopantetheine and uncompetitive versus ATP, binding to the enzyme-ATP complex, overview. The potency of the series is optimized using structure-based design, resulting in inhibition of cell growth of Gram-positive species. Levels of inhibitory activity of compounds against Staphylococcus aureus PPAT are measured in the forward direction, MIC values, mechanism of inhibition, overview
-
additional information
compound library screening, the potency of the series is optimized using structure-based design, resulting in inhibition of cell growth of Gram-positive species. Levels of inhibitory activity of compounds against Streptococcus mutans PPAT are measured in the reverse direction, MIC values, overview
-
additional information
ccompound library screening, mode-of-inhibition studies with Streptococcus pneumoniae PPAT demonstrate representatives of this series to be reversible inhibitors competitive versus phosphopantetheine and uncompetitive versus ATP, binding to the enzyme-ATP complex, overview. The potency of the series is optimized using structure-based design, resulting in inhibition of cell growth of Gram-positive species, killing kinetic assays using Staphylococcus aureus strains ARC516 and a LytA- for Streptococcus pneumoniae. Levels of inhibitory activity of compounds against Streptococcus pneumoniae PPAT are measured in the forward direction. MIC values, mechanism of inhibition, overview
-
additional information
-
compound library screening, the potency of the series is optimized using structure-based design, resulting in inhibition of cell growth of Gram-positive species. MIC values, overview
-
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0.00033 - 0.005
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
0.000098 - 0.0088
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
0.00025
(2S)-2-(3-chlorophenyl)-2-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]ethyl carbamate
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.000056 - 0.000064
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
0.000056 - 0.000064
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
0.000037 - 0.000049
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
0.0000011 - 0.0000054
(3R)-3-(3-chlorophenyl)-3-[(7-[[2-(3,5-dimethyl-1H-pyrazol-4-yl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
0.000004 - 0.0000043
(3R)-3-([7-[(1-acetyl-2,3-dihydro-1H-indol-5-yl)amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl]amino)-3-(3-chlorophenyl)propanenitrile
0.0000012 - 0.0000078
1-[5-[(2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-7-yl)amino]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
0.000000065 - 0.024
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
0.000051
2-[(1S)-2-(4-chlorophenyl)cyclopentyl]-1H-benzimidazol-4-ol
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00004 - 0.0095
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
0.000091
2-[1-(4-chlorophenyl)pyrrolidin-2-yl]-1H-benzimidazol-4-ol
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00025
2-[2-(4-chlorophenyl)ethyl]-1H-benzimidazol-4-ol
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00024
2-[[(1R)-1-(3-chlorophenyl)-3-hydroxypropyl]amino]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0009
2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-ethyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00025
2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00055
2-[[(1S)-1-(3-chlorophenyl)-2-hydroxyethyl]amino]-5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7(4H)-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00045
3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanamide
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0002
3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanoic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.000051
3-[(2S)-2-(4-hydroxy-1H-benzimidazol-2-yl)cyclopentyl]benzoic acid
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00000013 - 0.2
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
0.0000032 - 0.0000082
3-[4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-1-(methoxycarbonyl)piperidin-4-yl]propanoic acid
0.00032
5-(4-hydroxy-1H-benzimidazol-2-yl)-1-methyl-6-phenylpiperidin-2-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.038
CoA
Arabidopsis thaliana
-
-
0.027
L-ascorbate
Acinetobacter baumannii
pH not specified in the publication, temperature not specified in the publication
0.0000025 - 0.0000093
methyl (R)-4-(3-(2-cyano-1-((5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino)ethyl)benzyl)piperidine-1-carboxylate
0.0000051 - 0.000013
methyl 4-(2-cyanoethyl)-4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]piperidine-1-carboxylate
0.0000024 - 0.0000093
methyl 4-(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]benzene-1-sulfonyl)piperidine-1-carboxylate
0.0000088 - 0.00001
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-(3-hydroxypropyl)piperidine-1-carboxylate
0.0000049 - 0.0000081
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[(Z)-(methoxyimino)methyl]piperidine-1-carboxylate
0.0000075 - 0.000024
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[[(2-hydroxyethyl)amino]methyl]piperidine-1-carboxylate
0.0000027 - 0.0000082
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)sulfanyl]piperidine-1-carboxylate
0.00019
N-[(1R)-1-(3-chlorophenyl)ethyl]-5-methyl-1H-imidazo[4,5-b]pyridin-2-amine
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
-
0.00041
N-[(1R)-1-(3-chlorophenyl)ethyl]-5-methyl[1,3]thiazolo[4,5-b]pyridin-2-amine
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.00041
N2-[(1R)-1-(3-chlorophenyl)ethyl]-5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidine-2,7-diamine
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.03
PTX040334
Escherichia coli
-
IC50: 0.03 mM
0.000006
PTX042695
Escherichia coli
-
IC50: 0.000006 mM
0.000018
Sodium citrate
Acinetobacter baumannii
pH not specified in the publication, temperature not specified in the publication
0.00033
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Staphylococcus aureus
-
pH 7.0, 22°C, recombinant enzyme
0.00086
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Haemophilus influenzae
pH 7.0, 22°C, recombinant enzyme
0.005
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Homo sapiens
pH 7.0, 22°C, recombinant enzyme
0.000098
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Streptococcus mutans
pH 7.0, 22°C, recombinant enzyme
0.000205
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Streptococcus pneumoniae
pH 7.0, 22°C, recombinant enzyme
0.0073
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Staphylococcus aureus
-
pH 7.0, 22°C, recombinant enzyme
0.0088
(1S,2S)-N-(3-chlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Haemophilus influenzae
pH 7.0, 22°C, recombinant enzyme
0.000056
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
Escherichia coli
pH 7.5, temperature not specified in the publication
0.000064
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.000056
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.000064
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.000037
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.000049
(3R)-3-(3-chlorophenyl)-3-[(5-methyl-7-oxo-4,7-dihydro[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)amino]propanenitrile
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.0000011
(3R)-3-(3-chlorophenyl)-3-[(7-[[2-(3,5-dimethyl-1H-pyrazol-4-yl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000054
(3R)-3-(3-chlorophenyl)-3-[(7-[[2-(3,5-dimethyl-1H-pyrazol-4-yl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]propanenitrile
Escherichia coli
pH 7.5, temperature not specified in the publication
0.000004
(3R)-3-([7-[(1-acetyl-2,3-dihydro-1H-indol-5-yl)amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl]amino)-3-(3-chlorophenyl)propanenitrile
Escherichia coli
pH 7.5, temperature not specified in the publication
0.0000043
(3R)-3-([7-[(1-acetyl-2,3-dihydro-1H-indol-5-yl)amino]-5-methyl-1H-imidazo[4,5-b]pyridin-2-yl]amino)-3-(3-chlorophenyl)propanenitrile
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000012
1-[5-[(2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-7-yl)amino]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000078
1-[5-[(2-[[(1R)-1-(3-chlorophenyl)ethyl]amino]-5-methyl-1H-imidazo[4,5-b]pyridin-7-yl)amino]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
Escherichia coli
pH 7.5, temperature not specified in the publication
0.000000065
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
Streptococcus pneumoniae
pH 7.0, 22°C, recombinant enzyme
0.00000087
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
Staphylococcus aureus
-
pH 7.0, 22°C, recombinant enzyme
0.0000026
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
Streptococcus mutans
pH 7.0, 22°C, recombinant enzyme
0.00011
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
Escherichia coli
pH 7.0, 22°C, recombinant enzyme
0.00012
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
Haemophilus influenzae
pH 7.0, 22°C, recombinant enzyme
0.024
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
Homo sapiens
pH 7.0, 22°C, recombinant enzyme
0.00004
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
Streptococcus pneumoniae
pH 7.0, 22°C, recombinant enzyme
0.00049
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
Staphylococcus aureus
-
pH 7.0, 22°C, recombinant enzyme
0.0048
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
Escherichia coli
pH 7.0, 22°C, recombinant enzyme
0.0095
2-[(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)sulfanyl]-1H-imidazole-5-carboxylic acid
Haemophilus influenzae
pH 7.0, 22°C, recombinant enzyme
0.00000013
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
Streptococcus pneumoniae
pH 7.0, 22°C, recombinant enzyme
0.00000041
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
Staphylococcus aureus
-
pH 7.0, 22°C, recombinant enzyme
0.00033
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
Escherichia coli
pH 7.0, 22°C, recombinant enzyme
0.00074
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
Haemophilus influenzae
pH 7.0, 22°C, recombinant enzyme
0.2
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
Homo sapiens
pH 7.0, 22°C, recombinant enzyme
0.0000032
3-[4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-1-(methoxycarbonyl)piperidin-4-yl]propanoic acid
Escherichia coli
pH 7.5, temperature not specified in the publication
0.0000082
3-[4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-1-(methoxycarbonyl)piperidin-4-yl]propanoic acid
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000025
methyl (R)-4-(3-(2-cyano-1-((5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino)ethyl)benzyl)piperidine-1-carboxylate
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000093
methyl (R)-4-(3-(2-cyano-1-((5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino)ethyl)benzyl)piperidine-1-carboxylate
Escherichia coli
pH 7.5, temperature not specified in the publication
0.0000051
methyl 4-(2-cyanoethyl)-4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]piperidine-1-carboxylate
Escherichia coli
pH 7.5, temperature not specified in the publication
0.000013
methyl 4-(2-cyanoethyl)-4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]piperidine-1-carboxylate
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000024
methyl 4-(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]benzene-1-sulfonyl)piperidine-1-carboxylate
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000093
methyl 4-(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]benzene-1-sulfonyl)piperidine-1-carboxylate
Escherichia coli
pH 7.5, temperature not specified in the publication
0.0000088
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-(3-hydroxypropyl)piperidine-1-carboxylate
Escherichia coli
pH 7.5, temperature not specified in the publication
0.00001
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-(3-hydroxypropyl)piperidine-1-carboxylate
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000049
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[(Z)-(methoxyimino)methyl]piperidine-1-carboxylate
Escherichia coli
pH 7.5, temperature not specified in the publication
0.0000081
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[(Z)-(methoxyimino)methyl]piperidine-1-carboxylate
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000075
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[[(2-hydroxyethyl)amino]methyl]piperidine-1-carboxylate
Escherichia coli
pH 7.5, temperature not specified in the publication
0.000024
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)methyl]-4-[[(2-hydroxyethyl)amino]methyl]piperidine-1-carboxylate
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000027
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)sulfanyl]piperidine-1-carboxylate
Pseudomonas aeruginosa
pH 7.5, temperature not specified in the publication
0.0000082
methyl 4-[(3-[(1R)-2-cyano-1-[(5-methyl-1H-imidazo[4,5-b]pyridin-2-yl)amino]ethyl]phenyl)sulfanyl]piperidine-1-carboxylate
Escherichia coli
pH 7.5, temperature not specified in the publication
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in complex with sodium citrate, to 1.76 A resolution. Citrate binds at the ATP binding site
structures in complex with dephospho coenzyme A and coenzyme A, to 1.96 and 2.04 A resolution, respectively. Both bind in the substrate binding site
sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M sodium acetate pH 4.6, 30% (w/v) PEG 2000
ligand-unbound state and in complex with ATP and pantetheine, using 3.5 M sodium formate and 100 mM Tris-HCl (pH 8.5)
-
The best crystals are grown with a reservoir solution consisting of 0.1 M sodium HEPES pH 7.5, 0.8 M sodium dihydrogen phosphate, and 0.8 M potassium dihydrogen phosphate. Tetragonal bipyramidal crystals grew to approximate dimensions of 0.1 x 0.1 x 0.1 mm within a few days.
-
at pH 5.0, 100 mM sodium acetate, pH 5.0, 1.1 M ammonium sulfate, 200 mM NaCl
-
co-crystallization with CoA, space group: I23, with a dimer in the asymmetric unit, a solvent content of 0.57 and a volume-to-protein mass ratio of 288 A3 Da-1
co-crystallization with inhibitor PTX040334 in 5% DMSO, 22-32% polyethylene glycol 8000, 200 mM ammonium sulfate in 100 mM cacodylate buffer, pH 6-6.5 at 21°C
-
co-crystallization with pantetheine 4'-phosphate or ATP, space group: I23, with a dimer in the asymmetric unit, a solvent content of 57% and a volume-to-protein mass ratio of 288 A3 Da-1
in complex with inhibitors
hanging drop vapor diffusion method, using 0.1 M TrisHCl, pH 7.0, containing 2.0 M (NH4)2SO4 and 0.2 M Li2SO4
hanging-drop vapour-diffusion method, using sodium chloride as precipitant, trigonal space group P3121 or P3221 with six monomers in the asymmetric unit, a solvent content of 49% and a volume-to-protein mass ratio of 2.39 A3 Da-1
-
apo form and in complex with ATP, counter-diffusion method, using 40 mM cacodylate buffer pH 5.5 containing 10 mM MgCl2, 0.15 mM NaCl, 20 mM cobalt hexamine and 15% (w/v) 2-methyl-2,4-pentanediol as precipitant solution
enzyme crystals are grown in microgravity by the capillary counter-diffusion method through a gel layer, mixing of 10 mg/ml protein in 10 mM HEPES, pH 8.0, 0.15 M NaCl, and 14 mM ATP, with reservoir solution containing 0.1 M NaAc, pH 5.0, 10 mM MgCl2, 5 mM HEPES, pH 8.0, 0.075 M NaCl, 14 mM ATP, and 1.1 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement method
enzyme in complex with pantetheine 4'-phosphate and adenosine-5'-[(alpha,beta)-methyleno]triphosphate, sitting drop vapor diffusion method, using 38% (v/v) polyethylene glycol 200 and 0.1 M HEPES (pH 7.2), at 21°C
hanging drop vapor diffusion method
-
in complex with coenzyme A, hanging drop vapor diffusion method, using 0.1 M Tris base pH 8.0 and 0.15 M magnesium formate
-
space groups R32 and S32 using using 2-methyl-2,4-pentanediol or ammonium sulfate as the precipitant, respectively. Enzyme molecules in the crystals with space group P32 are more closely packed, and the access to the active site of the enzyme is restricted by intermolecular contacts. The independent hexameric molecule in the crystals with space group P32 forms a larger number of intermolecular polar contacts
-
purified recombinant His-tagged enzyme in complex with diphosphate, substrate analogue AMPPNP, and inhibitors acetyl-CoA and CoA, sitting drop vapor diffusion method, mixing of 0.002 ml of protein in 25 mM HEPES, pH 7.0, 300 mM NaCl, and 2% glycerol, with 0.002 ml of well solution containing 17-19% PEG 4000, 0.1 M HEPES, pH 6.8-7.2, 200-350 mM Na-acetate, and 5-7% 2-propanol, 3-4 weeks, 42°C, method optimization, crystals are soaked in 0.1 mM ligand solution, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
structure of apo-PPAT. Residues R90 and D94 residues act like a gate near the binding cavity to accommodate and stabilize the incoming ligand
enzyme from Staphylococcus aureus subsp. aureus MW2 in complex with inhibitors, vapour diffusion method, mixing of 0.0025 ml of protein solution with 0.0025 ml of reservoir solution containing 14% to 19% PEG 3350, 200 mM ammonium sulfate, and 0.1 M propionic acid cacodylate Bis-Tris propane buffer, pH 7.5, 20°C, 5-7 days, X-ray diffraction structure determination and analysis at 1.72-2.38 A resolution, molecular replacement and modelling of inhibitor binding
-
hanging-drop vapour-diffusion method, 23.85°C
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Brohn, F.H.; Trager, W.
Coenzyme A requirement of malaria parasites: enzymes of coenzyme A biosynthesis in normal duck erythrocytes and erythrocytes infected with Plasmodium lophurae
Proc. Natl. Acad. Sci. USA
72
2456-2458
1975
Anas sp., no activity in Plasmodium lophurae
brenda
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Mechanism of coenzyme A biosynthesis by Sarcina lutea
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95-99
1983
Micrococcus luteus
-
brenda
Hoagland, M.B.; Novelli, G.D.
Biosynthesis of coenzyme A from phosphopantetheine from pantothenate
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207
767-773
1954
Columba sp., Rattus norvegicus, Sus scrofa
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Enzymatic synthesis and structure of CoA
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12
675-681
1953
Columba sp., Sus scrofa
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Abiko, Y.
Pantothenic acid and coenzyme A: dephospho-CoA pyrophosphorylase and dephospho-CoA kinase as a possible bifunctional enzyme complex (ATP: pantetheine-4'-phosphate adenylyltransferase, ec 2.7.7.3 and ATP: dehospho-CoA 3'phosphotransferase, ec 2.7.1.24)
Methods Enzymol.
18A
358-364
1970
Rattus norvegicus
-
brenda
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A bifunctional enzyme complex in coenzyme A biosynthesis: purification of pantetheine phosphate adenylyltransferase and dephospho-CoA kinase
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215
153-157
1983
Rattus norvegicus, Sus scrofa
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Limited proteolysis of pig liver CoA synthase: evidence for subunit identity
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Rattus norvegicus, Sus scrofa
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Mitochondrial biosynthesis of coenzyme A
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91
1536-1542
1979
Rattus norvegicus
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Mitochondrial pantetheinephosphate adenylyltransferase and dephospho-CoA kinase
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131
57-63
1983
Rattus norvegicus
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Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase
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192
1155-1161
1993
Corynebacterium ammoniagenes
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Inhibitors of phosphopantetheine adenylyltransferase
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38
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2003
Escherichia coli, Sus scrofa
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A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A
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185
4074-4080
2003
Escherichia coli (P0A6I6)
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The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism
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315
487-495
2002
Escherichia coli (P0A6I6), Escherichia coli
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Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli
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274
27105-27111
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Escherichia coli
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Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori
Acta Crystallogr. Sect. D
59
561-562
2003
Helicobacter pylori
brenda
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Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase)
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365
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2002
Homo sapiens (Q13057), Homo sapiens, Sus scrofa (Q8MIR4), Sus scrofa
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Identification, purification, and characterization of an eukaryotic-like phosphopantetheine adenylyltransferase (coenzyme A biosynthetic pathway) in the hyperthermophilic archaeon Pyrococcus abyssi
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278
31078-31087
2003
Pyrococcus abyssi
brenda
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Rhombohedral crystals of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase
Acta Crystallogr. Sect. D
60
195-196
2004
Mycobacterium tuberculosis, Mycobacterium tuberculosis Rv2965c
brenda
Takahashi, H.; Inagaki, E.; Fujimoto, Y.; Kuroishi, C.; Nodake, Y.; Nakamura, Y.; Arisaka, F.; Yutani, K.; Kuramitsu, S.; Yokoyama, S.; Yamamoto, M.; Miyano, M.; Tahirov, T.H.
Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus
Acta Crystallogr. Sect. D
60
97-104
2004
Escherichia coli, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Nalezkova, M.; de Groot, A.; Graf, M.; Gans, P.; Blanchard, L.
Overexpression and purification of Pyrococcus abyssi phosphopantetheine adenylyltransferase from an optimized synthetic gene for NMR studies
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39
296-306
2005
Pyrococcus abyssi (Q9UYT0), Pyrococcus abyssi
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Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase
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13
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2004
Mycobacterium tuberculosis
brenda
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Overexpression, crystallization and preliminary X-ray crystallographic analysis of phosphopantetheine adenylyltransferase from Enterococcus faecalis
Acta Crystallogr. Sect. F
62
1131-1133
2006
Enterococcus faecalis
brenda
Miller, J.R.; Ohren, J.; Sarver, R.W.; Mueller, W.T.; de Dreu, P.; Case, H.; Thanabal, V.
Phosphopantetheine adenylyltransferase from Escherichia coli: Investigation of the kinetic mechanism and role in regulation of CoA biosynthesis
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189
8196-8205
2007
Escherichia coli
brenda
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The coenzyme a biosynthetic enzyme phosphopantetheine adenylyltransferase plays a crucial role in plant growth, salt/osmotic stress resistance, and seed lipid storage
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148
546-556
2008
Arabidopsis thaliana
brenda
Lee, H.H.; Yoon, H.J.; Kang, J.Y.; Park, J.H.; Kim, d.o..J.; Choi, K.H.; Lee, S.K.; Song, J.; Kim, H.J.; Suh, S.W.
The structure of Staphylococcus aureusphosphopantetheine adenylyltransferase in complex with 3-phosphoadenosine 5-phosphosulfate reveals a new ligand-binding mode
Acta Crystallogr. Sect. F
65
987-991
2009
Staphylococcus aureus (P63819), Staphylococcus aureus
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Timofeev, V.; Smirnova, E.; Chupova, L.; Esipov, R.; Kuranova, I.
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction
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68
1660-1670
2012
Mycobacterium tuberculosis (P9WPA5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPA5)
brenda
Edwards, T.E.; Leibly, D.J.; Bhandari, J.; Statnekov, J.B.; Phan, I.; Dieterich, S.H.; Abendroth, J.; Staker, B.L.; Van Voorhis, W.C.; Myler, P.J.; Stewart, L.J.
Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei
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67
1032-1037
2011
Burkholderia pseudomallei (Q3JW91), Burkholderia pseudomallei
brenda
Wubben, T.; Mesecar, A.D.
Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation
Acta Crystallogr. Sect. F
67
541-545
2011
Mycobacterium tuberculosis
brenda
Cheng, C.S.; Chen, C.H.; Luo, Y.C.; Chen, W.T.; Chang, S.Y.; Lyu, P.C.; Kao, M.C.; Yin, H.S.
Crystal structure and biophysical characterisation of Helicobacter pylori phosphopantetheine adenylyltransferase
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408
356-361
2011
Helicobacter pylori (O26010), Helicobacter pylori
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Substitution of asparagine 76 by a tyrosine residue induces domain swapping in Helicobacter pylori phosphopantetheine adenylyltransferase
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30
488-502
2012
Helicobacter pylori
brenda
Wubben, T.J.; Mesecar, A.D.
Kinetic, thermodynamic, and structural insight into the mechanism of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis
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404
202-219
2010
Mycobacterium tuberculosis (P9WPA5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPA5)
brenda
Yoon, H.J.; Kang, J.Y.; Mikami, B.; Lee, H.H.; Suh, S.W.
Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine
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32
431-435
2011
Enterococcus faecalis
brenda
de Jonge, B.L.; Walkup, G.K.; Lahiri, S.D.; Huynh, H.; Neckermann, G.; Utley, L.; Nash, T.J.; Brock, J.; San Martin, M.; Kutschke, A.; Johnstone, M.; Laganas, V.; Hajec, L.; Gu, R.F.; Ni, H.; Chen, B.; Hutchings, K.; Holt, E.; McKinney, D.; Gao, N.; Livchak, S.; Thresher, J.
Discovery of inhibitors of 4-phosphopantetheine adenylyltransferase (PPAT) to validate PPAT as a target for antibacterial therapy
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57
6005-6015
2013
Enterococcus faecium, Staphylococcus aureus, Streptococcus pyogenes, Candida albicans (B9WCR8), Escherichia coli (P0A6I6), Haemophilus influenzae (P44805), Homo sapiens (Q06203), Streptococcus pneumoniae (Q8DNE6), Streptococcus mutans (Q8DVH2), Enterococcus faecium ARC521, Streptococcus pyogenes ARC838, Haemophilus influenzae KW20 (P44805), Streptococcus mutans UA159 (Q8DVH2), Staphylococcus aureus RN4220
brenda
Chatterjee, R.; Mondal, A.; Basu, A.; Datta, S.
Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa
Biochim. Biophys. Acta
1864
773-786
2016
Pseudomonas aeruginosa (Q9I6D1), Pseudomonas aeruginosa
brenda
Timofeev, V.; Chupova, L.; Esipov, R.; Kuranova, I.
Crystallization and preliminary X-ray diffraction study of phosphopantetheine adenylyltransferase from M. tuberculosis crystallizing in space group P3_2
Crystallogr. Rep.
60
682-684
2015
Mycobacterium tuberculosis (P9WPA5)
-
brenda
Cheng, C.S.; Jia, K.F.; Chen, T.; Chang, S.Y.; Lin, M.S.; Yin, H.S.
Experimentally validated novel inhibitors of Helicobacter pylori phosphopantetheine adenylyltransferase discovered by virtual high-throughput screening
PLoS ONE
8
e74271
2013
Helicobacter pylori (O26010), Helicobacter pylori
brenda
Gupta, A.; Singh, P.K.; Iqbal, N.; Sharma, P.; Baraigya, H.R.; Kaur, P.; Umar, M.S.; Ahmad, F.; Sharma, A.; Owais, M.; Sharma, S.; Singh, T.P.
Structural and binding studies of phosphopantetheine adenylyl transferase from Acinetobacter baumannii
Biochim. Biophys. Acta
1867
537-547
2019
Acinetobacter baumannii (B0VTH7), Acinetobacter baumannii, Acinetobacter baumannii SDF (B0VTH7)
brenda
Podshivalov, D.; Timofeev, V.; Sidorov-Biryukov, D.; Kuranova, I.
Virtual screening of selective inhibitors of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis
Crystallogr. Rep.
62
405-410
2017
Mycobacterium tuberculosis (P9WPA5), Mycobacterium tuberculosis H37Rv (P9WPA5)
-
brenda
Timofeev, V.; Zhukhlistova, N.; Kuranova, I.
Crystal packing of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis in two crystal modifications
Crystallogr. Rep.
65
84-90
2020
Mycobacterium tuberculosis, Mycobacterium tuberculosis BT1
-
brenda
Gupta, A.; Singh, P.K.; Sharma, P.; Kaur, P.; Sharma, S.; Singh, T.P.
Structural and biochemical studies of phosphopantetheine adenylyltransferase from Acinetobacter baumannii with dephospho-coenzyme A and coenzyme A
Int. J. Biol. Macromol.
142
181-190
2020
Acinetobacter baumannii (B0VTH7), Acinetobacter baumannii, Acinetobacter baumannii SDF (B0VTH7)
brenda
Wang, Y.; Feng, S.; Gao, H.; Wang, J.
Computational investigations of gram-negative bacteria phosphopantetheine adenylyltransferase inhibitors using 3D-QSAR, molecular docking and molecular dynamic simulations
J. Biomol. Struct. Dyn.
38
1435-1447
2020
Escherichia coli (P0A6I6)
brenda
Moreau, R.J.; Skepper, C.K.; Appleton, B.A.; Blechschmidt, A.; Balibar, C.J.; Benton, B.M.; Drumm, J.E.; Feng, B.Y.; Geng, M.; Li, C.; Lindvall, M.K.; Lingel, A.; Lu, Y.; Mamo, M.; Mergo, W.; Polyakov, V.; Smith, T.M.; Takeoka, K.; Uehara, K.; Wang, L.; Wei, J.R.; Weiss, A.H.; Xie, L.; Xu, W.; Zhang, Q.; de Vicente, J.
Fragment-based drug discovery of inhibitors of phosphopantetheine adenylyltransferase from Gram-negative bacteria
J. Med. Chem.
61
3309-3324
2018
Escherichia coli (P0A6I6), Escherichia coli, Pseudomonas aeruginosa (Q9I6D1), Pseudomonas aeruginosa
brenda
Skepper, C.K.; Moreau, R.J.; Appleton, B.A.; Benton, B.M.; Drumm, J.E.; Feng, B.Y.; Geng, M.; Hu, C.; Li, C.; Lingel, A.; Lu, Y.; Mamo, M.; Mergo, W.; Mostafavi, M.; Rath, C.M.; Steffek, M.; Takeoka, K.T.; Uehara, K.; Wang, L.; Wei, J.R.; Xie, L.; Xu, W.; Zhang, Q.; de Vicente, J.
Discovery and optimization of phosphopantetheine adenylyltransferase inhibitors with Gram-negative antibacterial activity
J. Med. Chem.
61
3325-3349
2018
Escherichia coli (P0A6I6), Pseudomonas aeruginosa (Q9I6D1)
brenda
Mondal, A.; Chatterjee, R.; Datta, S.
Umbrella sampling and X-ray crystallographic analysis unveil an Arg-Asp gate facilitating inhibitor binding inside phosphopantetheine adenylyltransferase allosteric cleft
J. Phys. Chem. B
122
1551-1559
2018
Pseudomonas aeruginosa (A0A0X1KGP2), Pseudomonas aeruginosa, Pseudomonas aeruginosa 2192 (A0A0X1KGP2)
brenda