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ATP + (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
ADP + 4'-phospho-CJ-15,801
CJ-15,801, the compound is phosphorylated by pantothenate kinase (PanK). Subsequently, phospho-CJ-15,801 is accepted as a substrate by the next enzyme in the pathway (phosphopantothenoylcysteine synthetase, PPCS), and reacts to become cytidylylated. The cytidylylated phospho-CJ-15,801, which closely mimics the natural reaction intermediate and binds tightly and reversibly to the enzyme, does not react further and instead inhibits the enzyme
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-oxo-3-[[(piperidin-4-yl)methyl]amino]propyl)butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[(3-oxo-3-[[(piperidin-4-yl)methyl]amino]propyl)amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-oxo-3-[[2-(piperazin-1-yl)ethyl]amino]propyl)butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[(3-oxo-3-[[2-(piperazin-1-yl)ethyl]amino]propyl)amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-oxo-3-[[2-(pyridin-2-yl)ethyl]amino]propyl)butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[(3-oxo-3-[[2-(pyridin-2-yl)ethyl]amino]propyl)amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-[[2-oxo-2-(pentylamino)ethyl]amino]propyl)butanamide
ADP + N2-(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propyl)-N-pentylglycinamide
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-[[3-(morpholin-4-yl)propyl]amino]-3-oxopropyl)butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-[(3-[[3-(morpholin-4-yl)propyl]amino]-3-oxopropyl)amino]-4-oxobutyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[(1-pentyl-1H-1,2,3-triazol-4-yl)methyl]butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[[(1-pentyl-1H-1,2,3-triazol-4-yl)methyl]amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-(1-propyl-1H-1,2,3-triazol-4-yl)propyl]butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[[3-(1-propyl-1H-1,2,3-triazol-4-yl)propyl]amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-(pentylamino)propyl]butanamide
ADP + N3-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-pentyl-beta-alaninamide
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-(phenylamino)propyl]butanamide
ADP + N3-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-phenyl-beta-alaninamide
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-(pyrimidin-4-ylamino)propyl]butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-([3-oxo-3-[(pyrimidin-4-yl)amino]propyl]amino)butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(3-phenylpropyl)amino]propyl]butanamide
ADP + N3-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(3-phenylpropyl)-beta-alaninamide
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(pyridin-2-ylmethyl)amino]propyl]butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[(3-oxo-3-[[(pyridin-2-yl)methyl]amino]propyl)amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(pyridin-3-ylmethyl)amino]propyl]butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[(3-oxo-3-[[(pyridin-3-yl)methyl]amino]propyl)amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(pyridin-4-ylmethyl)amino]propyl]butanamide
ADP + (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-[(3-oxo-3-[[(pyridin-4-yl)methyl]amino]propyl)amino]butyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-[(3-methylpyridin-2-yl)amino]-3-oxopropyl]butanamide
ADP + (3R)-4-([3-[(3-aminopyridin-2-yl)amino]-3-oxopropyl]amino)-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-2,4-dihydroxy-N-(3-[[3-(1H-imidazol-1-yl)propyl]amino]-3-oxopropyl)-3,3-dimethylbutanamide
ADP + (3R)-3-hydroxy-4-[(3-[[3-(1H-imidazol-1-yl)propyl]amino]-3-oxopropyl)amino]-2,2-dimethyl-4-oxobutyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-N-[3-(1,3-dihydro-2H-isoindol-2-yl)-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
ADP + (3R)-4-[[3-(1,3-dihydro-2H-isoindol-2-yl)-3-oxopropyl]amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-N-[3-(2,3-dihydro-1H-indol-1-yl)-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
ADP + (3R)-4-[[3-(2,3-dihydro-1H-indol-1-yl)-3-oxopropyl]amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen phosphate
-
-
-
?
ATP + (2R)-N-[3-(benzylamino)-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
ADP + N-benzyl-N3-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide
-
-
-
?
ATP + (2R)-N-[3-[(2-butanamidoethyl)amino]-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
ADP + N-(2-butanamidoethyl)-N3-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide
-
-
-
?
ATP + (2S)-2-hydroxy-3-(hydroxymethyl)-3-methyl-N-[3-oxo-3-(pentylamino)propyl]pentanamide
ADP + N3-[(2S,3S)-2-hydroxy-3-methyl-3-[(phosphonooxy)methyl]pentanoyl]-N-pentyl-beta-alaninamide
-
-
-
?
ATP + (2S)-3-ethyl-2-hydroxy-3-(hydroxymethyl)-N-[3-oxo-3-(pentylamino)propyl]hept-6-ynamide
ADP + N3-[(2S,3S)-3-ethyl-2-hydroxy-3-[(phosphonooxy)methyl]hept-6-ynoyl]-N-pentyl-beta-alaninamide
-
-
-
?
ATP + (2S)-3-ethyl-2-hydroxy-3-(hydroxymethyl)-N-[3-oxo-3-(pentylamino)propyl]hex-5-enamide
ADP + N3-[(2S)-3-ethyl-2-hydroxy-3-[(phosphonooxy)methyl]hex-5-enoyl]-N-pentyl-beta-alaninamide
-
-
-
?
ATP + (2S)-3-ethyl-2-hydroxy-3-(hydroxymethyl)-N-[3-oxo-3-(pentylamino)propyl]pentanamide
ADP + N3-[(2S)-3-ethyl-2-hydroxy-3-[(phosphonooxy)methyl]pentanoyl]-N-pentyl-beta-alaninamide
-
-
-
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
the enzyme is involved in coenzyme A biosynthesis in the archaea
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
ATP + 3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]-2-(pentylamino)propanoate
ADP + 3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]-2-(pentylamino)propanoate
-
-
-
?
ATP + D-pantothenate
ADP + 4'-phosphopantothenate
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
ATP + N-alkylpantothenamides
ADP + ?
growth-inhibiting anti-metabolite, modeling into the active site structure
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
ATP + N-nonylpantothenamide
ADP + N-nonylpantothenamide 4-phosphate
ATP + N-pentylpantothenamide
ADP + N-pentylpantothenamide 4-phosphate
ATP + N-[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]-beta-alanyl-N-pentylglycinamide
ADP + N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl-N-pentylglycinamide
-
-
-
?
ATP + pantheteine
?
-
-
-
?
ATP + pantothenate
?
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
ATP + pantothenate
ADP + (R)-4-phosphopantothenate
-
-
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
ATP + pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
-
?
ATP + pantothenol
ADP + 4'-phosphopantothenol
CTP + (R)-pantothenate
CDP + (R)-4'-phosphopantothenate
dATP + (R)-pantothenate
dADP + (R)-4'-phosphopantothenate
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
GTP + pantothenate
GDP + D-4'-phosphopantothenate
ITP + pantothenate
IDP + D-4'-phosphopantothenate
-
phosphorylation at 46% the rate of ATP
-
-
?
pantetheine + ATP
D-4'-phosphopantetheine + ADP
-
-
-
-
?
panthenoylcysteine + ATP
D-4'-phosphopanthenoylcysteine + ADP
-
-
-
-
?
pantothenate + ATP
4'-phosphopantothenate + ADP
pantothenate + ATP
phosphopantothenate + ADP
pantothenate + CTP
4'-phosphopantothenate + CDP
-
-
-
-
?
pantothenate + dATP
4'-phosphopantothenate + dADP
-
-
-
-
?
pantothenate + dCTP
4'-phosphopantothenate + dCDP
-
-
-
-
?
pantothenate + dGTP
4'-phosphopantothenate + dGDP
-
-
-
-
?
pantothenate + dTTP
4'-phosphopantothenate + dTDP
-
-
-
-
?
pantothenate + UTP
4'-phosphopantothenate + UDP
-
-
-
-
?
pantothenyl alcohol + ATP
D-4'-phosphopantothenyl alcohol + ADP
-
-
-
-
?
polyphosphate(n) + (R)-pantothenate
polyphosphate(n-1) + (R)-4'-phosphopantothenate
-
-
-
?
UTP + (R)-pantothenate
UDP + (R)-4'-phosphopantothenate
-
-
-
?
UTP + pantothenate
UDP + D-4'-phosphopantothenate
-
phosphorylation at 18% the rate of ATP
-
-
?
additional information
?
-
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
coaX is essential for growth of Bacillus anthracis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
the enzyme is absolutely specific for ATP, no activity with CTP, GTP, UTP, or phosphoenolpyruvate as phosphoryl donors
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
first step in coenzyme A biosynthesis, the enzyme has a regulatory function in the pathway
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
pantothenate binding site structure involving residues E249, Y262, F247, F259, Y258, and F244, located at the distal end of a large surface groove, induced fit binding mechanism, overview
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
the phosphate binding loop of isozyme mPanK2 is the N-terminal motif DIGGT(S)XXK
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis, regulatory function
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
i.e. vitamin B5
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
i.e. vitamin B5
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
A0A167Z3Z6
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
A0A167Z3Z6
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
ir
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
ir
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + D-pantothenate
ADP + 4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + 4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
poor phosphate donor: alpha,beta-methyleneadenosine 5'-triphosphate
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
transfers the gamma-phosphate of ATP to pantothenate
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
first and rate-controlling reaction of CoA-biosynthesis
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
D-configuration of 2'-hydroxyl group in pantothenate molecule is essential for functional interaction with enzyme
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
first and rate-controlling reaction of CoA-biosynthesis
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
-
-
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
-
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
-
-
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
-
substrate is converted to the inactive butyldethia-CoA analogue in the further downstream pathway leading to grwoth inhibition of the organism, overview
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
-
-
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
-
substrate is converted to the inactive butyldethia-CoA analogue in the further downstream pathway leading to grwoth inhibition of the organism, overview
-
-
?
ATP + N-nonylpantothenamide
ADP + N-nonylpantothenamide 4-phosphate
-
-
-
?
ATP + N-nonylpantothenamide
ADP + N-nonylpantothenamide 4-phosphate
-
-
-
?
ATP + N-pentylpantothenamide
ADP + N-pentylpantothenamide 4-phosphate
-
-
-
?
ATP + N-pentylpantothenamide
ADP + N-pentylpantothenamide 4-phosphate
-
-
-
-
?
ATP + N-pentylpantothenamide
ADP + N-pentylpantothenamide 4-phosphate
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
-
first step of the pathway from pantothenate to CoA. The activity of this protein is tightly regulated by CoA feedback inhibition, both in vitro and in vivo
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
-
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
pantothenate kinase catalyzes the first step in CoA biosynthesis
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
-
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
-
-
-
?
ATP + pantothenol
ADP + 4'-phosphopantothenol
-
-
-
?
ATP + pantothenol
ADP + 4'-phosphopantothenol
-
-
-
?
CTP + (R)-pantothenate
CDP + (R)-4'-phosphopantothenate
-
-
-
?
CTP + (R)-pantothenate
CDP + (R)-4'-phosphopantothenate
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
-
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
-
-
-
?
GTP + pantothenate
GDP + D-4'-phosphopantothenate
-
phosphorylation at 28% the rate of ATP
-
-
?
GTP + pantothenate
GDP + D-4'-phosphopantothenate
-
phosphorylation at 20% the rate of ATP
-
-
?
pantothenate + ATP
4'-phosphopantothenate + ADP
-
-
-
-
?
pantothenate + ATP
4'-phosphopantothenate + ADP
-
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
-
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
relative activity with GTP: 81%, CTP: 68%, and UTP: 91.8%
-
-
?
additional information
?
-
-
type III PanK in the spore-forming Bacillus anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen
-
-
?
additional information
?
-
type III PanK in the spore-forming Bacillus anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen
-
-
?
additional information
?
-
-
N-pentylpantothenate is no substrate
-
-
?
additional information
?
-
EhPanK utilizes various nucleoside triphosphates, ATP, CTP, GTP, UTP, dATP, and polyphosphates, as well as deoxynucleotides as phosphoryl donors, with ATP being the best phosphate donor
-
-
-
additional information
?
-
-
EhPanK utilizes various nucleoside triphosphates, ATP, CTP, GTP, UTP, dATP, and polyphosphates, as well as deoxynucleotides as phosphoryl donors, with ATP being the best phosphate donor
-
-
-
additional information
?
-
no acivity with hopantenate, formation of a pantothenate kinase-ADP-pantothenate ternary complex
-
-
?
additional information
?
-
-
no acivity with hopantenate, formation of a pantothenate kinase-ADP-pantothenate ternary complex
-
-
?
additional information
?
-
N-pentylpantothenate is no substrate, no activity with UTP or phosphoenolpyruvate as phosphoryl donors
-
-
?
additional information
?
-
-
N-pentylpantothenate is no substrate, no activity with UTP or phosphoenolpyruvate as phosphoryl donors
-
-
?
additional information
?
-
-
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
-
-
?
additional information
?
-
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
-
-
?
additional information
?
-
-
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
-
-
?
additional information
?
-
-
miRNAs, which exist in vertebrate genomes within introns of the pantothenate kinase genes, are predicted by bioinformatics to affect multiple mRNA targets in pathways that involve cellular acetyl-CoA and lipid levels. Significantly, PANK enzymes also affect these pathways, so the miRNA and host gene may act synergistically. These predictions require experimental verification
-
-
?
additional information
?
-
-
pantothenate kinase is upregulated in the warming treatment
-
-
?
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(2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
(2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
-
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
(2R)-2,4-dihydroxy-3,3-dimethylbutanohydrazide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-2,4-dihydroxy-N-(2-hydroxyethyl)-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-N-(2,3-dihydroxypropyl)-2,4-dihydroxy-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
(2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
-
(2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
-
(R)-3-azido-4,4-dimethyl-dihydro-furan-2-one
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
(R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
(R)-4-(2-azido-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
(S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
(S)-trifluoro-methanesulfonic acid 4,4-dimethyl-2-oxo-tetrahydro-furan-3-yl-ester
1,4-dioxa-8-azaspiro[4.5]dec-8-yl[2-[(3-fluorophenyl)sulfanyl]pyridin-4-yl]methanone
-
mixed non-competitive inhibition
1,4-phenylene-bis(1,2-ethanediyl)bis-isothiourea dihydrobromide
-
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
2,6-difluoro-N-[1-(5-[[2-(4-fluorophenoxy)ethyl]sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl)ethyl]benzamide
competitive inhibition
2-chloro-N-[1-(5-[[2-(4-fluorophenoxy)ethyl]sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl)ethyl]benzamide
competitive inhibition
2-[(4'-cyano-2-[[4-(pyridin-2-yl)piperazin-1-yl]methyl][1,1'-biphenyl]-4-yl)oxy]-1-oxoethan-1-aminide
non-competitive inhibition
2-[2-(1-benzoylpiperidin-4-yl)-5-methyl-1,3-thiazol-4-yl]-N-(4-methylphenyl)acetamide
-
uncompetitive inhibition
4-(2,4-dihydroxy-3,3-dimethylbutylamido)butyric acid
-
competitive inhibitor; competitive inhibitor, IC50: 0.05-0.15 mM
4-phosphopantoate
substrate inhibition
5'-deoxy-5'-(4-(beta-D-galactopyranosyloxymethyl)-1,2,3-triazol-1-yl)adenosine
-
competitive inhibitor with respect to ATP
benzyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
benzyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
benzyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
benzyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
CoA esters
-
feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2
D-pantothenate
-
substrate inhibition, above 0.5 mM
dehydroisoandrosterone
about 30% residual activity at 0.1 mM (isoform PanK3)
Dehydroisoandrosterone sulfate
about 8% residual activity at 0.1 mM (isoform PanK3)
ephedrine hydrochloride
-
estradiol
about 80% residual activity at 0.1 mM (isoform PanK3)
Estradiol sulfate
about 90% residual activity at 0.1 mM (isoform PanK3)
Estrone sulfate
about 50% residual activity at 0.1 mM (isoform PanK3)
ethyl (2E)-2-methyl-3-[[(4R)-2,2,5,5-tetramethyl-1,3-dioxane-4-carbonyl]amino]prop-2-enoate
-
ethyl (2E)-3-(2-oxoazepan-1-yl)prop-2-enoate
-
ethyl (2E)-3-(2-oxoazocan-1-yl)prop-2-enoate
-
ethyl (2E)-3-(2-oxoazonan-1-yl)prop-2-enoate
-
ethyl (2E)-3-benzamido-2-methylprop-2-enoate
-
ethyl (2E)-3-benzamidoprop-2-enoate
-
ethyl (2E)-3-[(pyridine-3-carbonyl)amino]prop-2-enoate
-
ethyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]-2-methylprop-2-enoate
-
ethyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
ethyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
ethyl (2E)-3-[[(4R)-2,2,5,5-tetramethyl-1,3-dioxane-4-carbonyl]amino]prop-2-enoate
-
ethyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
ethyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
malonyl CoA
competitive versus ATP, uncompetitive versus pantothenate
MCC-555
MCC-555 inhibits all three isoforms with a rank order of PanK3 > PanK2 > PanK1b; MCC-555 inhibits all three isoforms with a rank order of PanK3 > PanK2 > PanK1b
methyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
methyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
methyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
methyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
N-(1-[5-[(4-fluorobenzyl)sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl]ethyl)-2-(trifluoromethyl)benzamide
competitive inhibition
N-(2-(benzo[d][1,3]dioxol-5-yl)ethyl)pantothenamide
A0A167Z3Z6
-
N-(3-methoxyphenethyl)pantothenamide
A0A167Z3Z6
-
N-(5-methoxypentyl)pantothenamide
A0A167Z3Z6
-
N-(benzo[d][1,3]dioxol-5-ylmethyl)pantothenamide
A0A167Z3Z6
-
N-phenethylpantothenamide
A0A167Z3Z6
-
N-[1-(5-[[2-(4-chlorophenoxy)ethyl]sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl)ethyl]naphthalene-1-carboxamide
-
competitive inhibition
N-[1-(5-[[2-(4-fluorophenoxy)ethyl]sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl)ethyl]-2-(trifluoromethyl)benzamide
competitive inhibition
N-[1-(5-[[2-(4-fluorophenoxy)ethyl]sulfanyl]-4-[(4-fluorophenyl)methyl]-4H-1,2,4-triazol-3-yl)ethyl]-2-(trifluoromethyl)benzamide
competitive inhibition
pantothenamide
A0A167Z3Z6
-
pantothenamide, N-substituted
-
IC50 about 0.0004-0.0016 mM
-
pantothenic acid 4'-phosphate
-
-
pantothenol
-
competitive inhibition
pantothenoylcysteine 4'-phosphate
pioglitazone hydrochloride
-
pregnenolone sulfate
about 10% residual activity at 0.1 mM (isoform PanK3); about 92% residual activity at 0.1 mM (isoform PanK3)
tert-butyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
tert-butyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
tert-butyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
tert-butyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
-
[(4'-cyano-2-[[4-(pyridin-2-yl)piperazin-1-yl]methyl][1,1'-biphenyl]-4-yl)oxy]acetic acid
non-competitive inhibition
[2-[(3-chlorophenyl)sulfanyl]pyridin-4-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
-
mixed non-competitive inhibition
[2-[(3-chlorophenyl)sulfanyl]quinolin-4-yl](piperidin-1-yl)methanone
-
mixed non-competitive inhibition
[[2-[[4-(6-methylpyridin-2-yl)piperazin-1-yl]methyl]-4'-(trifluoromethoxy)biphenyl-4-yl]oxy]acetic acid
-
mixed non-competitive inhibition
(2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
CJ-15,801, an enamide analogue of pantothenate isolated from the fungus Seimatosporium sp. CL28611. CJ-15,801 is phosphorylated by pantothenate kinase (PanK). Subsequently, phospho-CJ-15,801 is accepted as a substrate by the next enzyme in the pathway (phosphopantothenoylcysteine synthetase, PPCS), and reacts to become cytidylylated. The cytidylylated phospho-CJ-15,801, which closely mimics the natural reaction intermediate and binds tightly and reversibly to the enzyme, does not react further and instead inhibits the enzyme
(2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
-
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(R)-3-azido-4,4-dimethyl-dihydro-furan-2-one
-
-
(R)-3-azido-4,4-dimethyl-dihydro-furan-2-one
-
-
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
80.6% inhibition at 0.1 mM, purified enzyme
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
29.4% inhibition at 0.1 mM, purified enzyme
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
2.7% inhibition at 0.1 mM, cell extract
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
78.7% inhibition at 0.1 mM, purified enzyme
(R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
11% inhibition at 0.1 mM, purified enzyme
(R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
13.1% inhibition at 0.1 mM, cell extract
(R)-4-(2-azido-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
-
(R)-4-(2-azido-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
-
(S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
12.5% inhibition at 0.1 mM, purified enzyme
(S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
54.6% inhibition at 0.1 mM, purified enzyme
(S)-trifluoro-methanesulfonic acid 4,4-dimethyl-2-oxo-tetrahydro-furan-3-yl-ester
-
-
(S)-trifluoro-methanesulfonic acid 4,4-dimethyl-2-oxo-tetrahydro-furan-3-yl-ester
-
-
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
10.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
76.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
89.6% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
98.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
46.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
71.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
89.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
97.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
12.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
72.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
81.4% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
98.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
59.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
57.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
80.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
89.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
51.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
82.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
86.8% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
99.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
40.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
71.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
84.6% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
86.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
35.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
44.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
70.5% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
17.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
28.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
33.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
57.4% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
8.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
71.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
3.0% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
93.3% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
76.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
41.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
28.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
68.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
95.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
61.0% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
53.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
82.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
97.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
49.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
61.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
85.0% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
96.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
13.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
10.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
39.1% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
4.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
92.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
90.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
98.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
97.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
62.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
32.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
61.2% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
96.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
72.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
54.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
87.2% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
97.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
54.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
55.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
82.2% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
53.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
15.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
7.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
73.0% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
9.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
25.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
3.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
56.7% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
72.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
26.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
28.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
67.6% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
90.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 36.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 11.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 70.3% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 79.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
52.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
38.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
64.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
94.4% inhibition at 0.1 mM, purified enzyme
acetyl-CoA
selective and strong, competitive to ATP
acetyl-CoA
mixed-type inhibition versus pantothenate and ATP
acetyl-CoA
competitive inhibitor of purified PanK2 with respect to ATP; IC50: 60 nM, competitive inhibitor with respect to ATP
acetyl-CoA
a feedback inhibitor; a feedback inhibitor
acetyl-CoA
complete inhibition of isoform PanK3 at 0.008 mM
acetyl-CoA
feedback inhibition, competitive versus ATP, but acetyl-CoA binds far more tightly than ATP. The 1alpha and 1beta isoforms are least sensitive to inhibition, whereas isoforms 2 and 3 are more potently inhibited by acetyl-CoA; feedback inhibition, competitive versus ATP, but acetyl-CoA binds far more tightly than ATP. The 1alpha and 1beta isoforms are least sensitive to inhibition, whereas isoforms 2 and 3 are more potently inhibited by acetyl-CoA; feedback inhibition, competitive versus ATP, but acetyl-CoA binds far more tightly than ATP. The 1alpha and 1beta isoforms are least sensitive to inhibition, whereas isoforms 2 and 3 are more potently inhibited by acetyl-CoA
acetyl-CoA
-
feedback inhibition, regulatory function, isozyme PanK1beta and isozyme PanK3, strong inhibition of mutant chimera PanK1beta-3-1beta, slight inhibition of mutant chimera PanK3-1beta-3
acetyl-CoA
feedback inhibition, competitive versus ATP, but acetyl-CoA binds far more tightly than ATP. The 1alpha and 1beta isoforms are least sensitive to inhibition, whereas isoforms 2 and 3 are more potently inhibited by acetyl-CoA; feedback inhibition, competitive versus ATP, but acetyl-CoA binds far more tightly than ATP. The 1alpha and 1beta isoforms are least sensitive to inhibition, whereas isoforms 2 and 3 are more potently inhibited by acetyl-CoA; feedback inhibition, competitive versus ATP, but acetyl-CoA binds far more tightly than ATP. The 1alpha and 1beta isoforms are least sensitive to inhibition, whereas isoforms 2 and 3 are more potently inhibited by acetyl-CoA. Comparison of the overall structures of the actyl-CoA-bound inactive and the active PANK3 conformations, overview
acetyl-CoA
-
effective inhibitor
Acyl carrier protein
-
-
Acyl carrier protein
-
PAK II: inhibition, PAK I: stimulation between 0.015-0.035 mM
acyl-CoA-esters
long chain acyl CoA, feed-back inhibition, isoform PanK1alpha
acyl-CoA-esters
-
long-chain acyl-CoAs less efficient than short-chain ester
ADP
-
not
ADP
competitive inhibitor of isoform PanK3 with respect to ATP1 and a mixed-type inhibitor with respect to pantothenate
ATP
-
free form
CoA
-
not
CoA
competitive versus ATP, uncompetitive versus pantothenate
CoA
-
in vitro; in vivo; kinetics
CoA
-
feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2
CoA
feed-back inhibition, isoform PanK1alpha
CoA
feedback inhibition, Tm values of wild-type and its mutants and dissociation constants of CoA, overview
CoA
-
not reversible by D-carnitine, acetyl-L-carnitine or other carnitine analogs; reversible by L-carnitine
CoA
-
feed-back inhibition; in vitro; reversible by L-carnitine
CoA
-
inhibits isoform A stronger than isoform B
coenzyme A
allosteric regulator, feedback inhibition
coenzyme A
-
feedback inhibition, regulatory function, isozyme PanK1beta, slight inhibition of isozyme PanK3
coenzyme A
-
feedback inhibition regulates pantothenol uptake. Furosemide reduces this inherent feedback inhibition by competing with coenzyme A for binding to pantothenate kinase, thereby increasing pantothenol uptake
dephospho-CoA
-
-
malonyl-CoA
-
-
malonyl-CoA
-
feedback inhibition, regulatory function, isozyme PanK3, slight inhibition of isozyme PanK1beta
malonyl-CoA
-
effective inhibitor
malonyl-CoA
-
0.075 mM, complete inhibition of PAK I
N-heptylpantothenamide
-
-
N-heptylpantothenamide
competitive to pantothenate
N-heptylpantothenamide
-
IC50 is 0.0048 mM, potent growth inhibitory anti-metabolite
N-heptylpantothenamide
A0A167Z3Z6
-
N-pentylpantothenamide
-
-
N-pentylpantothenamide
competitive to pantothenate
N-pentylpantothenamide
-
IC50 is 0.0035 mM, has antimicrobial activity against Staphylococcus aureus
N-pentylpantothenamide
A0A167Z3Z6
-
palmitoyl-CoA
-
-
palmitoyl-CoA
strong inhibitor
palmitoyl-CoA
-
feedback inhibition, regulatory function, isozyme PanK3, mutant chimera PanK1beta-3-1beta, slight inhibition of mutant chimera PanK3-1beta-3
pantetheine 4'-phosphate
-
weak
pantetheine 4'-phosphate
-
not
pantetheine 4'-phosphate
-
strong
pantothenoylcysteine 4'-phosphate
-
weak
pantothenoylcysteine 4'-phosphate
-
strong
additional information
-
no inhibition by (R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid and (S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview
-
additional information
-
the enzyme is not subject to feedback inhibition by CoASH
-
additional information
the enzyme is not subject to feedback inhibition by CoASH
-
additional information
-
no inhibition by N-pentylpantothenamide, enzyme is not affected by CoA or acetyl-CoA
-
additional information
-
no inhibition by 2,2'-dipyridyl, Ca2+, Cd2+, 3'-AMP, GTP, GDP, ITP, UTP; not inhibitory: 3',5'-ADP
-
additional information
inhibitor library screening and evaluation of cytotoxicity against human fibroblast MRC-5 cells. IC50 values for cytotoxicity against Entamoeba trophozoites and human MRC-5 cells, overview
-
additional information
-
inhibitor library screening and evaluation of cytotoxicity against human fibroblast MRC-5 cells. IC50 values for cytotoxicity against Entamoeba trophozoites and human MRC-5 cells, overview
-
additional information
-
not inhibitory: 3',5'-ADP; not inhibitory: cAMP, NADH, NADPH, CoA:glutathione disulfide; not inhibitory: NAD+
-
additional information
-
structural features required for enzyme inhibition, overview
-
additional information
no inhibition by hopantenate
-
additional information
-
no inhibition by hopantenate
-
additional information
-
inhibition by CoA thioesters
-
additional information
no inhibition by N-pentylpantothenamide, enzyme is not affected by CoA or acetyl-CoA
-
additional information
-
no inhibition by N-pentylpantothenamide, enzyme is not affected by CoA or acetyl-CoA
-
additional information
-
feedback inhibition by acyl-CoAs
-
additional information
-
isoform PanK3 is not inhibited by estrone
-
additional information
isoform PanK3 is not inhibited by estrone
-
additional information
-
no inhibition by (S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview
-
additional information
-
structural determinants for feedback inhibition
-
additional information
-
in vivo antiplasmodial activities of the inhibitor molecules, overview
-
additional information
structure-activity analysis of (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid (CJ-15,801) analogues that interact with Plasmodium falciparum pantothenate kinase and inhibit parasite proliferation. Inhibitor selectivity, overview. The enamide analogues of pantothenate may inhibit pantothenate phosphorylation by one of two mechanisms: (i) by directly inhibiting PfPanK, or (ii) by serving as alternate substrates that are competitively phosphorylated. It is noteworthy that the IC50 value of the best pantothenate phosphorylation inhibitor is 13fold lower than the pantothenate concentration present in the assay (0.0018 mM). Assuming competition for the same binding site, this is consistent with the enamide binding PanK with higher affinity and/or being turned over more slowly than the natural substrate. Effect of pantothenate supplementation on the antiplasmodial activity of CJ-15,801 and derivatives
-
additional information
-
structure-activity analysis of (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid (CJ-15,801) analogues that interact with Plasmodium falciparum pantothenate kinase and inhibit parasite proliferation. Inhibitor selectivity, overview. The enamide analogues of pantothenate may inhibit pantothenate phosphorylation by one of two mechanisms: (i) by directly inhibiting PfPanK, or (ii) by serving as alternate substrates that are competitively phosphorylated. It is noteworthy that the IC50 value of the best pantothenate phosphorylation inhibitor is 13fold lower than the pantothenate concentration present in the assay (0.0018 mM). Assuming competition for the same binding site, this is consistent with the enamide binding PanK with higher affinity and/or being turned over more slowly than the natural substrate. Effect of pantothenate supplementation on the antiplasmodial activity of CJ-15,801 and derivatives
-
additional information
-
not inhibitory: Mg2+, NADP+; not inhibitory: NAD+
-
additional information
-
not inhibitory: 3',5'-ADP; not inhibitory: CoASH, acetyl-CoA
-
additional information
-
no inhibition by (R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview
-
additional information
-
no feedback regulation by CoA or acetyl-CoA
-
additional information
A0A167Z3Z6
the potent antistaphylococcal activity of N-substituted pantothenamides (PanAms) exhibit inhibition of Staphylococcus aureus atypical type II pantothenate kinase (SaPanKII). The PanAms are phosphorylated by SaPanKII but remain bound at the active site. This occurs primarily through interactions with Tyr240' and Thr172'. Kinetic analysis shows a strong correlation between kcat (slow PanAm turnover) and IC50 (inhibition of pantothenate phosphorylation) values, suggesting that SaPanKII inhibition occurs via a delay in product release. The two PanAms, N-(benzo[d][1,3]dioxol-5-ylmethyl)pantothenamide and N-(5-methoxypentyl)pantothenamide, effectively combine both hydrogen bonding and hydrophobic interactions, resulting in the most potent SaPanKII inhibition described to date. Design and synthesis of a series of N-substituted pantothenamides, analysis of the PanAm binding mode and interaction with the N-substituent binding site, structure-activity realtionships, MIC values, overview
-
additional information
-
the potent antistaphylococcal activity of N-substituted pantothenamides (PanAms) exhibit inhibition of Staphylococcus aureus atypical type II pantothenate kinase (SaPanKII). The PanAms are phosphorylated by SaPanKII but remain bound at the active site. This occurs primarily through interactions with Tyr240' and Thr172'. Kinetic analysis shows a strong correlation between kcat (slow PanAm turnover) and IC50 (inhibition of pantothenate phosphorylation) values, suggesting that SaPanKII inhibition occurs via a delay in product release. The two PanAms, N-(benzo[d][1,3]dioxol-5-ylmethyl)pantothenamide and N-(5-methoxypentyl)pantothenamide, effectively combine both hydrogen bonding and hydrophobic interactions, resulting in the most potent SaPanKII inhibition described to date. Design and synthesis of a series of N-substituted pantothenamides, analysis of the PanAm binding mode and interaction with the N-substituent binding site, structure-activity realtionships, MIC values, overview
-
additional information
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
-
additional information
-
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
-
additional information
-
not inhibited by CoA or its thioesters
-
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1
(2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-oxo-3-[[(piperidin-4-yl)methyl]amino]propyl)butanamide
at pH 7.6, temperature not specified in the publication
1
(2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-oxo-3-[[2-(piperazin-1-yl)ethyl]amino]propyl)butanamide
at pH 7.6, temperature not specified in the publication
0.11
(2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-oxo-3-[[2-(pyridin-2-yl)ethyl]amino]propyl)butanamide
at pH 7.6, temperature not specified in the publication
1.2
(2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-[[2-oxo-2-(pentylamino)ethyl]amino]propyl)butanamide
at pH 7.6, temperature not specified in the publication
0.35
(2R)-2,4-dihydroxy-3,3-dimethyl-N-(3-[[3-(morpholin-4-yl)propyl]amino]-3-oxopropyl)butanamide
at pH 7.6, temperature not specified in the publication
0.19
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[(1-pentyl-1H-1,2,3-triazol-4-yl)methyl]butanamide
at pH 7.6, temperature not specified in the publication
1
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-(1-propyl-1H-1,2,3-triazol-4-yl)propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.036
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-(pentylamino)propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.043
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-(phenylamino)propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.45
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-(pyrimidin-4-ylamino)propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.032
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(3-phenylpropyl)amino]propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.05
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(pyridin-2-ylmethyl)amino]propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.033
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(pyridin-3-ylmethyl)amino]propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.13
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-oxo-3-[(pyridin-4-ylmethyl)amino]propyl]butanamide
at pH 7.6, temperature not specified in the publication
0.039
(2R)-2,4-dihydroxy-3,3-dimethyl-N-[3-[(3-methylpyridin-2-yl)amino]-3-oxopropyl]butanamide
at pH 7.6, temperature not specified in the publication
0.022
(2R)-2,4-dihydroxy-N-(3-[[3-(1H-imidazol-1-yl)propyl]amino]-3-oxopropyl)-3,3-dimethylbutanamide
at pH 7.6, temperature not specified in the publication
0.2
(2R)-N-[3-(1,3-dihydro-2H-isoindol-2-yl)-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
at pH 7.6, temperature not specified in the publication
0.4
(2R)-N-[3-(2,3-dihydro-1H-indol-1-yl)-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
at pH 7.6, temperature not specified in the publication
0.067
(2R)-N-[3-(benzylamino)-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
at pH 7.6, temperature not specified in the publication
0.24
(2R)-N-[3-[(2-butanamidoethyl)amino]-3-oxopropyl]-2,4-dihydroxy-3,3-dimethylbutanamide
at pH 7.6, temperature not specified in the publication
0.23
(2S)-2-hydroxy-3-(hydroxymethyl)-3-methyl-N-[3-oxo-3-(pentylamino)propyl]pentanamide
at pH 7.6, temperature not specified in the publication
0.11
(2S)-3-ethyl-2-hydroxy-3-(hydroxymethyl)-N-[3-oxo-3-(pentylamino)propyl]hept-6-ynamide
at pH 7.6, temperature not specified in the publication
0.59 - 1.2
(2S)-3-ethyl-2-hydroxy-3-(hydroxymethyl)-N-[3-oxo-3-(pentylamino)propyl]hex-5-enamide
0.0057 - 0.833
(R)-pantothenate
0.7
3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]-2-(pentylamino)propanoate
at pH 7.6, temperature not specified in the publication
668
GTP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
0.008 - 0.124
N-heptylpantothenamide
0.003 - 0.14
N-pentylpantothenamide
0.12
N-[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]-beta-alanyl-N-pentylglycinamide
at pH 7.6, temperature not specified in the publication
0.06
pantheteine
at pH 7.6, temperature not specified in the publication
additional information
additional information
-
0.59
(2S)-3-ethyl-2-hydroxy-3-(hydroxymethyl)-N-[3-oxo-3-(pentylamino)propyl]hex-5-enamide
at pH 7.6, temperature not specified in the publication
1.2
(2S)-3-ethyl-2-hydroxy-3-(hydroxymethyl)-N-[3-oxo-3-(pentylamino)propyl]hex-5-enamide
at pH 7.6, temperature not specified in the publication
0.0057
(R)-pantothenate
-
recombinant isozyme PanK1beta, pH 7.0, 37°C
0.009
(R)-pantothenate
-
recombinant isozyme iPanK2, pH 7.5, 37°C
0.0095
(R)-pantothenate
-
recombinant isozyme PanK3, pH 7.0, 37°C
0.014
(R)-pantothenate
isoform PanK3, at pH 7.5 and 37°C
0.017
(R)-pantothenate
pH 7.5, 37°C, wild-type enzyme
0.021
(R)-pantothenate
at pH 7.6, temperature not specified in the publication
0.023
(R)-pantothenate
-
pH 7.5, 37°C, recombinant enzyme
0.025
(R)-pantothenate
-
recombinant isozyme mPanK2, pH 7.5, 37°C
0.041
(R)-pantothenate
pH 7.5, 37°C, recombinant His-tagged enzyme
0.043
(R)-pantothenate
-
in 100 mM HEPES, pH 7.6, 20 mM KCl, 10 mM MgCl2, 2 mM phosphoenolpyruvate, 0.3 mM NADH, 5 units of lactate dehydrogenase, 2.5 units of pyruvate kinase, and 0.00027 mM of the PanK-III protein, at 50°C
0.0532
(R)-pantothenate
pH 6.0, 37°C, recombinant enzyme
0.101
(R)-pantothenate
pH 7.6, 25°C
0.168
(R)-pantothenate
-
pH 7.6, 25°C
0.833
(R)-pantothenate
pH 7.5, 37°C, mutant PanK3 R107W
0.0031
ATP
pH 7.5, 37°C, wild-type enzyme
0.025
ATP
pH 7.5, 37°C, mutant PanK3 R107W
0.034
ATP
-
pH 7.5, 37°C, recombinant enzyme
0.0414
ATP
pH 6.0, 37°C, recombinant enzyme
0.05
ATP
25°C, pH 7.8, determined by isothermal titration calorimetry
0.064
ATP
-
recombinant isozyme mPanK2, pH 7.5, 37°C
0.068
ATP
-
recombinant isozyme iPanK2, pH 7.5, 37°C
0.087
ATP
-
recombinant isozyme PanK1beta, pH 7.0, 37°C
0.112
ATP
-
recombinant isozyme PanK3, pH 7.0, 37°C
0.115
ATP
-
Tris-HCl buffer, pH 8.0
0.151
ATP
Tris-HCl buffer, pH8.0
0.225
ATP
-
ATP in form of MgATP2-
0.311
ATP
isoform PanK3, at pH 7.5 and 37°C
0.375
ATP
25°C, pH 7.8, determined from coupled assay
0.406
ATP
-
citrate buffer, pH 6.0
0.6
ATP
-
ATP in form of MgATP2-
0.616
ATP
citrate buffer, pH6.0
0.616
ATP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
1
ATP
-
ATP in form of MgATP2-
1
ATP
-
ATP in form of MgATP2-
6.04
ATP
-
in 100 mM HEPES, pH 7.6, 20 mM KCl, 10 mM MgCl2, 2 mM phosphoenolpyruvate, 0.3 mM NADH, 5 units of lactate dehydrogenase, 2.5 units of pyruvate kinase, and 0.00027 mM of the PanK-III protein, at 50°C
0.008
N-heptylpantothenamide
-
pH 7.5, 37°C, recombinant enzyme
0.124
N-heptylpantothenamide
pH 7.5, 37°C, recombinant His-tagged enzyme
0.003
N-pentylpantothenamide
-
pH 7.5, 37°C, recombinant enzyme
0.14
N-pentylpantothenamide
pH 7.5, 37°C, recombinant His-tagged enzyme
0.009
pantothenate
-
-
0.011
pantothenate
-
pH 6.1, 37°C
0.016
pantothenate
-
pH 6.1, 37°C
0.018
pantothenate
-
pH 7.0, 37°C
0.027
pantothenate
-
pH 7.5, 25°C
0.067
pantothenate
-
pH 6.5, 37°C
0.1
pantothenate
25°C, pH 7.8, determined from coupled assay
0.18
pantothenate
25°C, pH 7.8, determined by isothermal titration calorimetry
0.8
pantothenate
-
isoform 2, 37°C, pH 8.0
1.3
pantothenate
-
isoform 1, 37°C, pH 8.0
0.25
pantothenol
25°C, pH 7.8, determined by isothermal titration calorimetry
0.28
pantothenol
25°C, pH 7.8, determined from coupled assay
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics of recombinant isozyme mPanK2
-
additional information
additional information
-
allosteric regulation of mammalian pantothenate kinase
-
additional information
additional information
allosteric regulation of mammalian pantothenate kinase
-
additional information
additional information
allosteric regulation of mammalian pantothenate kinase
-
additional information
additional information
allosteric regulation of mammalian pantothenate kinase
-
additional information
additional information
allosteric regulation of mammalian pantothenate kinase
-
additional information
additional information
allosteric regulation of mammalian pantothenate kinase
-
additional information
additional information
-
allosteric regulation of mammalian pantothenate kinase
-
additional information
additional information
Michaelis-Menten kinetics. EhPanK exhibits hyperbolic saturation kinetics when assayed over the substrate range of 0.004-0.256 mM for pantothenate in the presence of 0.025-0.10 mM ATP and 0.001-0.10 mM ATP in the presence of 0.008-0.128 mM pantothenate
-
additional information
additional information
-
Michaelis-Menten kinetics. EhPanK exhibits hyperbolic saturation kinetics when assayed over the substrate range of 0.004-0.256 mM for pantothenate in the presence of 0.025-0.10 mM ATP and 0.001-0.10 mM ATP in the presence of 0.008-0.128 mM pantothenate
-
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0.2
(2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.1
(2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.036
(2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
Plasmodium falciparum
pH and temperature not specified in the publication
0.1
(2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.0084
1,4-dioxa-8-azaspiro[4.5]dec-8-yl[2-[(3-fluorophenyl)sulfanyl]pyridin-4-yl]methanone
Mycobacterium tuberculosis
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25°C
0.0004
1,4-phenylene-bis(1,2-ethanediyl)bis-isothiourea dihydrobromide
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.00257
2-[2-(1-benzoylpiperidin-4-yl)-5-methyl-1,3-thiazol-4-yl]-N-(4-methylphenyl)acetamide
Mycobacterium tuberculosis
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25°C
0.05 - 0.15
4-(2,4-dihydroxy-3,3-dimethylbutylamido)butyric acid
Mus musculus
-
competitive inhibitor, IC50: 0.05-0.15 mM
0.00006 - 0.000125
acetyl-CoA
0.089
benzyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.1
benzyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.013
benzyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.1
benzyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.2299
cephaloridine
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0059
chloranil
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.2
CoA
Plasmodium falciparum
-
IC50: 0.2 mM
0.0035
Dehydroisoandrosterone sulfate
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0778
echinomycin
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0016
ephedrine hydrochloride
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.1313
erythromycin A
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.093
ethyl (2E)-2-methyl-3-[[(4R)-2,2,5,5-tetramethyl-1,3-dioxane-4-carbonyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.181
ethyl (2E)-3-(2-oxoazepan-1-yl)prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.093
ethyl (2E)-3-(2-oxoazocan-1-yl)prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.061
ethyl (2E)-3-(2-oxoazonan-1-yl)prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.12
ethyl (2E)-3-benzamido-2-methylprop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.158
ethyl (2E)-3-benzamidoprop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.2
ethyl (2E)-3-[(pyridine-3-carbonyl)amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.2
ethyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]-2-methylprop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.159 - 0.2
ethyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
0.1
ethyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.144
ethyl (2E)-3-[[(4R)-2,2,5,5-tetramethyl-1,3-dioxane-4-carbonyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.159
ethyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.1
ethyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.3464
fluorescamine
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0001
Fusidic acid
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0492
gardimycin
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0052
glipizide
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0068
glyburide
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0092
GW5074
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0088
Hexachlorophene
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.1937
hygromycin A
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.2541
kasugamycin
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.2
methyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.1
methyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.2
methyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.1
methyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.02
N-(2-(benzo[d][1,3]dioxol-5-yl)ethyl)pantothenamide
Staphylococcus aureus
A0A167Z3Z6
pH 7.6, 25°C
0.01
N-(3-methoxyphenethyl)pantothenamide
Staphylococcus aureus
A0A167Z3Z6
pH 7.6, 25°C
0.00013
N-(5-methoxypentyl)pantothenamide
Staphylococcus aureus
A0A167Z3Z6
pH 7.6, 25°C
0.00046
N-(benzo[d][1,3]dioxol-5-ylmethyl)pantothenamide
Staphylococcus aureus
A0A167Z3Z6
pH 7.6, 25°C
0.0048 - 0.018
N-heptylpantothenamide
0.0035 - 0.006
N-pentylpantothenamide
0.036
N-phenethylpantothenamide
Staphylococcus aureus
A0A167Z3Z6
pH 7.6, 25°C
0.00007
N-[1-(5-[[2-(4-chlorophenoxy)ethyl]sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl)ethyl]naphthalene-1-carboxamide
Mycobacterium tuberculosis
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25°C
0.1472
neomycin
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.2838
O-methylnanaomycin A
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0004 - 0.0016
pantothenamide, N-substituted
Staphylococcus aureus
-
IC50 about 0.0004-0.0016 mM
-
0.001
pioglitazone hydrochloride
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0025
pregnenolone sulfate
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0016
Psi-rhodomyrtoxin
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0013
Reactive blue 2
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0039
Ro 41-0960
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.1657
rosamycin
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0017
rosiglitazone
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.1554
streptomycin
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0263
teicoplanin
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.039
tert-butyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.1
tert-butyl (2E)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.042
tert-butyl (2Z)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.1
tert-butyl (2Z)-3-[[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.2288
tirandamycin A
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.0092
tolfenamic acid
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.3099
trichostatin A
Entamoeba histolytica
recombinant enzyme, pH 6.0, 37°C
0.003
tyrphostin AG 528
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.009
tyrphostin AG 808
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0007
WIN 62577
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.00024 - 0.00042
[2-[(3-chlorophenyl)sulfanyl]pyridin-4-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
0.00087
[2-[(3-chlorophenyl)sulfanyl]quinolin-4-yl](piperidin-1-yl)methanone
Mycobacterium tuberculosis
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25°C
0.00082
[[2-[[4-(6-methylpyridin-2-yl)piperazin-1-yl]methyl]-4'-(trifluoromethoxy)biphenyl-4-yl]oxy]acetic acid
Mycobacterium tuberculosis
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25°C
0.00006
acetyl-CoA
Homo sapiens
IC50: 60 nM, competitive inhibitor with respect to ATP
0.0000625
acetyl-CoA
Mus musculus
-
-
0.000125
acetyl-CoA
Homo sapiens
-
-
0.159
ethyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
pH and temperature not specified in the publication
0.2
ethyl (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoate
Plasmodium falciparum
above, pH and temperature not specified in the publication
0.0048
N-heptylpantothenamide
Staphylococcus aureus
-
IC50 is 0.0048 mM, potent growth inhibitory anti-metabolite
0.018
N-heptylpantothenamide
Staphylococcus aureus
A0A167Z3Z6
pH 7.6, 25°C
0.0035
N-pentylpantothenamide
Staphylococcus aureus
-
IC50 is 0.0035 mM, has antimicrobial activity against Staphylococcus aureus
0.006
N-pentylpantothenamide
Staphylococcus aureus
A0A167Z3Z6
pH 7.6, 25°C
0.00024
[2-[(3-chlorophenyl)sulfanyl]pyridin-4-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
Mycobacterium tuberculosis
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25°C
0.00042
[2-[(3-chlorophenyl)sulfanyl]pyridin-4-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
Mycobacterium tuberculosis
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25°C
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evolution
comparison of MtPanK with the Escherichia coli enzyme EcPanK, overview. Despite the high sequence identity (52%) between EcPanK and MtPanK, the two enzymes differ in many respects, crystal structure comparison. While EcPanK is specific for ATP, MtPanK exhibits dual specificity and can make use of ATP as well as GTP for phosphorylating pantothenic acid. CoA binds nearly 40% more tightly to MtPanK than to EcPanK
evolution
isozyme PANK3 belongs to the ASKHA kinase superfamily, which typically uses either an Asp or Glu residue as the catalytic base to activate the substrate hydroxyl for attack on the gamma-phosphate of ATP
evolution
isozyme PANK3 belongs to the ASKHA kinase superfamily, which typically uses either an Asp or Glu residue as the catalytic base to activate the substrate hydroxyl for attack on the gamma-phosphate of ATP. Glu138 appears to be the logical candidate for the catalytic base
evolution
the human genome encodes three well-characterized and nearly identical pantothenate kinases (PANK1-3) plus a putative bifunctional protein (PANK4) with a predicted amino-terminal pantothenate kinase domain fused to a carboxy-terminal phosphatase domain. Structural and phylogenetic analyses show that all active, characterized PANKs contain the key catalytic residues Glu138 and Arg207 (HsPANK3 numbering). All amniote PANK4s, including human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity. Human PANK4 is a pseudo-pantothenate kinase, a catalytically deficient variant of the catalytically active PANK4 found in plants and fungi. Evolutionary history of PANK, phylogenetic analysis, overview
evolution
the human genome encodes three well-characterized and nearly identical pantothenate kinases (PANK1-3) plus a putative bifunctional protein (PANK4) with a predicted N-terminal pantothenate kinase domain fused to a C-terminal phosphatase domain. Structural and phylogenetic analyses show that all active, characterized PANKs contain the key catalytic residues Glu138 and Arg207 (HsPANK3 numbering). All amniote PANK4s, including human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity. Human PANK4 is a pseudo-pantothenate kinase, a catalytically deficient variant of the catalytically active PANK4 found in plants and fungi. Evolutionary history of PANK, overview
evolution
-
comparison of MtPanK with the Escherichia coli enzyme EcPanK, overview. Despite the high sequence identity (52%) between EcPanK and MtPanK, the two enzymes differ in many respects, crystal structure comparison. While EcPanK is specific for ATP, MtPanK exhibits dual specificity and can make use of ATP as well as GTP for phosphorylating pantothenic acid. CoA binds nearly 40% more tightly to MtPanK than to EcPanK
-
evolution
-
comparison of MtPanK with the Escherichia coli enzyme EcPanK, overview. Despite the high sequence identity (52%) between EcPanK and MtPanK, the two enzymes differ in many respects, crystal structure comparison. While EcPanK is specific for ATP, MtPanK exhibits dual specificity and can make use of ATP as well as GTP for phosphorylating pantothenic acid. CoA binds nearly 40% more tightly to MtPanK than to EcPanK
-
malfunction
disease: pantothenate kinase-associated neurodegeneration
malfunction
-
pantothenate kinase-associated neurodegeneration, formerly known as Hallervorden-Spatz syndrome
malfunction
-
flies carrying a fumble loss-of-function allele have a 3fold increase in total zinc levels per dry weight when compared to control strains, but no change in total iron, copper or manganese levels
malfunction
-
the elimination of PanK1 reduces hepatic CoA levels. Pank1-deficient mice become hypoglycemic during a fast due to impaired gluconeogenesis
malfunction
altered pantothenate utilization dramatically alters the susceptibility of yeast cells to ergosterol biosynthesis inhibitors. Inhibition of pantothenic acid utilization synergizes with the activity of the ergosterol molecule-targeting antifungal amphotericin B and antagonizes that of the ergosterol pathway-targeting antifungal drug terbinafine. Inhibition of pantothenate utilization results in reduced susceptibility to terbinafine and enhanced susceptibility to amphotericin B. Inhibition of Cab1p activity results in reduced squalene and lanosterol levels
malfunction
epigenetic gene silencing of PanK resulting in a significant reduction of PanK activity, intracellular CoA concentrations, and growth retardation in vitro, reinforcing the importance of this gene in Entamoeba histolytica
malfunction
human PANK3 is inactivated by mutations Glu138Val and Arg207Trp
malfunction
human PANK4 is a pseudo-pantothenate kinase, a catalytically deficient variant of the catalytically active PANK4 found in plants and fungi. Pank4 encodes Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity
malfunction
mutant Pank1-/-Pank2-/- double knock-out mice are unable to metabolize fats and ketones resulting in early postnatal death, and Pank1-/-Pank3-/- and Pank2-/- Pank-/- double knock-out mice are both embryonic lethal. A chemical knockout of all pantothenate kinases in adult mice results in an 80% reduction in hepatic CoA levels and death within days
malfunction
mutant Pank1-/-Pank2-/- double knock-out mice are unable to metabolize fats and ketones resulting in early postnatal death, and Pank1-/-Pank3-/- and Pank2-/- Pank-/-x03 double knock-out mice are both embryonic lethal. A chemical knockout of all pantothenate kinases in adult mice results in an 80% reduction in hepatic CoA levels and death within days
malfunction
mutant Pank1-/-Pank2-/- double knock-out mice are unable to metabolize fats and ketones resulting in early postnatal death, and Pank1-/-Pank3-/- and Pank2-/-Pank3-/- double knock-out mice are both embryonic lethal. A chemical knockout of all pantothenate kinases in adult mice results in an 80% reduction in hepatic CoA levels and death within days
malfunction
mutations in the pantothenate kinase of Plasmodium falciparum confer diverse sensitivity profiles to antiplasmodial pantothenate analogues. Pfpank1 mutations mediate parasite resistance to PanOH and CJ-15,801. Parasites pressured with pantothenol or (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid (CJ-15,801) become resistant to these antiplasmodial pantothenate analogues. Whole-genome sequencing reveals mutations in one of two putative PanK genes (Pfpank1) in each resistant line. These mutations significantly alter PfPanK activity, with two conferring a fitness cost, consistent with Pfpank1 coding for a functional PanK that is essential for normal growth. Different pantothenate analogue classes have different mechanisms of action: some inhibit CoA biosynthesis while others inhibit CoA-utilising enzymes
malfunction
structure-activity analysis of (2E)-3-[[(2R)-2,4-dihydroxy-3,3-dimethylbutanoyl]amino]prop-2-enoic acid (CJ-15,801) analogues that interact with Plasmodium falciparum pantothenate kinase and inhibit parasite proliferation. The conservation of the R-pantoyl moiety and the trans-substituted double bond of CJ-15,801 is important for the selective, on-target antiplasmodial effect, while replacement of the carboxyl group is permitted, and, in one case, favored. The antiplasmodial potency of CJ-15,801 analogues, that retain the R-pantoyl and trans-substituted enamide moieties, correlates with inhibition of Plasmodium falciparum pantothenate kinase (PfPanK)-catalyzed pantothenate phosphorylation
malfunction
A0A167Z3Z6
the potent antistaphylococcal activity of N-substituted pantothenamides (PanAms) exhibit inhibition of Staphylococcus aureus's atypical type II pantothenate kinase (SaPanKII), the first enzyme of coenzyme A biosynthesis. The mechanism of action follows from SaPanKII having a binding mode for PanAms that is distinct from those of other PanKs. Molecular interactions responsible for PanAm inhibitory activity, overview. The PanAms are phosphorylated by SaPanKII but remain bound at the active site, SaPanKII inhibition occurs via a delay in product release
malfunction
-
altered pantothenate utilization dramatically alters the susceptibility of yeast cells to ergosterol biosynthesis inhibitors. Inhibition of pantothenic acid utilization synergizes with the activity of the ergosterol molecule-targeting antifungal amphotericin B and antagonizes that of the ergosterol pathway-targeting antifungal drug terbinafine. Inhibition of pantothenate utilization results in reduced susceptibility to terbinafine and enhanced susceptibility to amphotericin B. Inhibition of Cab1p activity results in reduced squalene and lanosterol levels
-
malfunction
-
the potent antistaphylococcal activity of N-substituted pantothenamides (PanAms) exhibit inhibition of Staphylococcus aureus's atypical type II pantothenate kinase (SaPanKII), the first enzyme of coenzyme A biosynthesis. The mechanism of action follows from SaPanKII having a binding mode for PanAms that is distinct from those of other PanKs. Molecular interactions responsible for PanAm inhibitory activity, overview. The PanAms are phosphorylated by SaPanKII but remain bound at the active site, SaPanKII inhibition occurs via a delay in product release
-
metabolism
pantothenate kinase catalyzes the rate-controlling step in coenzyme A biosynthesis
metabolism
A0A167Z3Z6
CoA biosynthesis and salvage pathways, overview. The Staphylococcus aureus atypical type II pantothenate kinase (SaPanKII) is active in bothe pathways
metabolism
detailed metabolic pathway from pantothenate to ergosterol involving enzyme Cab1, overview
metabolism
four key enzymes are involved in the CoA pathway: pantothenate kinase (PanK, EC 2.7.1.33), bifunctional phosphopantothenate-cysteine ligase/decarboxylase (PPCS-PPCDC), phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA kinase (DPCK)
metabolism
PanK is the rate-limiting enzyme for CoA synthesis in Saccharomyces cerevisiae, acetyl-CoA metabolism and associated naringenin synthesis pathway overview
metabolism
the biosynthesis of CoA consists of five enzymatically catalysed steps, the first of which involves the conversion of vitamin B5 (pantothenate) to 4'-phosphopantothenate by ATP-mediated phosphorylation carried out by pantothenate kinase
metabolism
-
PanK is the rate-limiting enzyme for CoA synthesis in Saccharomyces cerevisiae, acetyl-CoA metabolism and associated naringenin synthesis pathway overview
-
metabolism
-
PanK is the rate-limiting enzyme for CoA synthesis in Saccharomyces cerevisiae, acetyl-CoA metabolism and associated naringenin synthesis pathway overview
-
metabolism
-
detailed metabolic pathway from pantothenate to ergosterol involving enzyme Cab1, overview
-
metabolism
-
the biosynthesis of CoA consists of five enzymatically catalysed steps, the first of which involves the conversion of vitamin B5 (pantothenate) to 4'-phosphopantothenate by ATP-mediated phosphorylation carried out by pantothenate kinase
-
metabolism
-
the biosynthesis of CoA consists of five enzymatically catalysed steps, the first of which involves the conversion of vitamin B5 (pantothenate) to 4'-phosphopantothenate by ATP-mediated phosphorylation carried out by pantothenate kinase
-
metabolism
-
CoA biosynthesis and salvage pathways, overview. The Staphylococcus aureus atypical type II pantothenate kinase (SaPanKII) is active in bothe pathways
-
physiological function
-
CoaA is essential for survival of Mycobacterium tuberculosis. The coax gene is unable to complement the loss of gene coaA. CoaX lacks pantothenate kinase activity in vitro and is not required for survival in macrophages and mice
physiological function
-
pantothenate kinase 1 is required to support the metabolic transition from the fed to the fasted state
physiological function
allosteric regulation of mammalian pantothenate kinase. Pantothenate kinase is the master regulator of CoA biosynthesis and is feedback-inhibited by acetyl-CoA
physiological function
allosteric regulation of mammalian pantothenate kinase. Pantothenate kinase is the master regulator of CoA biosynthesis and is feedback-inhibited by acetyl-CoA
physiological function
pantothenate kinase generates 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) biosynthesis. Critical roles of Glu138 and Arg207 in HsPANK3
physiological function
pantothenate kinase generates 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) biosynthesis. Isozyme PanK4 is a putative bifunctional protein with a predicted amino-terminal pantothenate kinase domain fused to a carboxy-terminal phosphatase domain. HsPANK4 has reduced kinase activity prior to the catalytic residue substitutions in amniotes. Human PANK4 is a pseudo-pantothenate kinase, a catalytically deficient variant of the catalytically active PANK4 found in plants and fungi
physiological function
pantothenate, the substrate for PanK and precursor for CoA, is directly related with acetyl-CoA biosynthesis in Saccharomyces cerevisiae. PanK is the rate-limiting step for CoA synthesis and pantothenate supplement helps to increase the CoA/acetyl-CoA level in mammalian and Escherichia coli cells, as well as in Saccharomyces cerevisiae cells
physiological function
the malaria-causing blood stage of Plasmodium falciparum requires extracellular pantothenate for proliferation. The parasite converts pantothenate into coenzyme A (CoA) via five enzymes, the first being a pantothenate kinase (PfPanK). Pfpank1 coding for a functional PanK that is essential for normal growth. Plasmodium falciparum parasites have previously been shown to survive equally well in a pantothenate-free complete RPMI 1640 medium supplemented with 0.1 mM CoA as compared to standard complete medium, consistent with them having the capacity to take up exogenous CoA, hence bypassing the need for any PfPanK activity
physiological function
the pantothenate kinase Cab1p catalyzes the first step in the metabolism of pantothenic acid for CoA biosynthesis in budding yeast (Saccharomyces cerevisiae), it significantly regulates the levels of sterol intermediates and the activities of ergosterol biosynthesis-targeting antifungals. This regulation is mediated by changes both in the expression of ergosterol biosynthesis genes and in the levels of sterol intermediates. The CoA metabolism controls ergosterol biosynthesis and susceptibility to antifungals
physiological function
-
pantothenate, the substrate for PanK and precursor for CoA, is directly related with acetyl-CoA biosynthesis in Saccharomyces cerevisiae. PanK is the rate-limiting step for CoA synthesis and pantothenate supplement helps to increase the CoA/acetyl-CoA level in mammalian and Escherichia coli cells, as well as in Saccharomyces cerevisiae cells
-
physiological function
-
CoaA is essential for survival of Mycobacterium tuberculosis. The coax gene is unable to complement the loss of gene coaA. CoaX lacks pantothenate kinase activity in vitro and is not required for survival in macrophages and mice
-
physiological function
-
pantothenate, the substrate for PanK and precursor for CoA, is directly related with acetyl-CoA biosynthesis in Saccharomyces cerevisiae. PanK is the rate-limiting step for CoA synthesis and pantothenate supplement helps to increase the CoA/acetyl-CoA level in mammalian and Escherichia coli cells, as well as in Saccharomyces cerevisiae cells
-
physiological function
-
the pantothenate kinase Cab1p catalyzes the first step in the metabolism of pantothenic acid for CoA biosynthesis in budding yeast (Saccharomyces cerevisiae), it significantly regulates the levels of sterol intermediates and the activities of ergosterol biosynthesis-targeting antifungals. This regulation is mediated by changes both in the expression of ergosterol biosynthesis genes and in the levels of sterol intermediates. The CoA metabolism controls ergosterol biosynthesis and susceptibility to antifungals
-
additional information
-
mitochondria-targeted human pantothenate kinase-2 is involved in pantothenate kinase-associated neurodegeneration
additional information
comparison of the human PANK3x02acetyl-CoA complex to the structures of PANK3 in four catalytically relevant complexes, 5'-adenylyl-beta,gamma-imidodiphosphate (AMPPNP)x02Mg2+, MPPNP-Mg2+-pantothenate, ADP-Mg2+-phosphopantothenate, and AMP phosphoramidate (AMPPN)-Mg2+, all reveal a large conformational change in the dimeric enzyme. The amino-terminal nucleotide binding domain rotates to close the active site, and this allows the P-loop to engage ATP and facilitates required substrate/product interactions at the active site. The transition between the inactive and active conformations, as assessed by the binding of either ATP-Mg2+ or acyl-CoA to PANK3, is highly cooperative indicating that both protomers move in concert. The communication between the two protomers is mediated by an alpha-helix that interacts with the ATP-binding site at its amino terminus and with the substrate/inhibitor-binding site of the opposite protomer at its carboxyl terminus. The two alpha-helices within the dimer together with the bound ligands create a ring that stabilizes the assembly in either the active closed conformation or the inactive open conformation. Thus, both active sites of the dimeric mammalian pantothenate kinases coordinately switch between the on and off states in response to intracellular concentrations of ATP and its key negative regulators, acetyl(acyl)-CoA. Analysis of PANK3 catalytic intermediates. Glu138 appears to be the logical candidate for the catalytic base, binding structure, and substrate/product interactions within the active site during the PANK3 catalytic cycle, detailed overview
additional information
comparison of the human PANK3x02acetyl-CoA complex to the structures of PANK3 in four catalytically relevant complexes, 5'-adenylyl-beta,gamma-imidodiphosphate (AMPPNP)x02Mg2+, MPPNP-Mg2+-pantothenate, ADP-Mg2+-phosphopantothenate, and AMP phosphoramidate (AMPPN)-Mg2+, all reveal a large conformational change in the dimeric enzyme. The amino-terminal nucleotide binding domain rotates to close the active site, and this allows the P-loop to engage ATP and facilitates required substrate/product interactions at the active site. The transition between the inactive and active conformations, as assessed by the binding of either ATP-Mg2+ or acyl-CoA to PANK3, is highly cooperative indicating that both protomers move in concert. The communication between the two protomers is mediated by an alpha-helix that interacts with the ATP-binding site at its amino terminus and with the substrate/inhibitor-binding site of the opposite protomer at its carboxyl terminus. The two alpha-helices within the dimer together with the bound ligands create a ring that stabilizes the assembly in either the active closed conformation or the inactive open conformation. Thus, both active sites of the dimeric mammalian pantothenate kinases coordinately switch between the on and off states in response to intracellular concentrations of ATP and its key negative regulators, acetyl(acyl)-CoA. Analysis of PANK3 catalytic intermediates. Glu138 appears to be the logical candidate for the catalytic base, binding structure, and substrate/product interactions within the active site during the PANK3 catalytic cycle, detailed overview
additional information
comparison of the human PANK3x02acetyl-CoA complex to the structures of PANK3 in four catalytically relevant complexes, 5'-adenylyl-beta,gamma-imidodiphosphate (AMPPNP)x02Mg2+, MPPNP-Mg2+-pantothenate, ADP-Mg2+-phosphopantothenate, and AMP phosphoramidate (AMPPN)-Mg2+, all reveal a large conformational change in the dimeric enzyme. The amino-terminal nucleotide binding domain rotates to close the active site, and this allows the P-loop to engage ATP and facilitates required substrate/product interactions at the active site. The transition between the inactive and active conformations, as assessed by the binding of either ATP-Mg2+ or acyl-CoA to PANK3, is highly cooperative indicating that both protomers move in concert. The communication between the two protomers is mediated by an alpha-helix that interacts with the ATP-binding site at its amino terminus and with the substrate/inhibitor-binding site of the opposite protomer at its carboxyl terminus. The two alpha-helices within the dimer together with the bound ligands create a ring that stabilizes the assembly in either the active closed conformation or the inactive open conformation. Thus, both active sites of the dimeric mammalian pantothenate kinases coordinately switch between the on and off states in response to intracellular concentrations of ATP and its key negative regulators, acetyl(acyl)-CoA. Analysis of PANK3 catalytic intermediates. Glu138 appears to be the logical candidate for the catalytic base, binding structure, and substrate/product interactions within the active site during the PANK3 catalytic cycle, detailed overview
additional information
-
comparison of the human PANK3x02acetyl-CoA complex to the structures of PANK3 in four catalytically relevant complexes, 5'-adenylyl-beta,gamma-imidodiphosphate (AMPPNP)x02Mg2+, MPPNP-Mg2+-pantothenate, ADP-Mg2+-phosphopantothenate, and AMP phosphoramidate (AMPPN)-Mg2+, all reveal a large conformational change in the dimeric enzyme. The amino-terminal nucleotide binding domain rotates to close the active site, and this allows the P-loop to engage ATP and facilitates required substrate/product interactions at the active site. The transition between the inactive and active conformations, as assessed by the binding of either ATP-Mg2+ or acyl-CoA to PANK3, is highly cooperative indicating that both protomers move in concert. The communication between the two protomers is mediated by an alpha-helix that interacts with the ATP-binding site at its amino terminus and with the substrate/inhibitor-binding site of the opposite protomer at its carboxyl terminus. The two alpha-helices within the dimer together with the bound ligands create a ring that stabilizes the assembly in either the active closed conformation or the inactive open conformation. Thus, both active sites of the dimeric mammalian pantothenate kinases coordinately switch between the on and off states in response to intracellular concentrations of ATP and its key negative regulators, acetyl(acyl)-CoA. Analysis of PANK3 catalytic intermediates. Glu138 appears to be the logical candidate for the catalytic base, binding structure, and substrate/product interactions within the active site during the PANK3 catalytic cycle, detailed overview
additional information
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sequence comparison of isozyme PanK3 and PanK4
additional information
sequence comparison of isozyme PanK3 and PanK4
additional information
the structure of PfPanK1 minus its parasite-specific inserts is predicted by homology modeling using the AMPPNP and pantothenate-bound human PanK3 structure (PDB ID 5KPR) as a template. PfPanK1 shares 28% sequence identity with human PanK3 over the protein parts that are modeled
additional information
-
the structure of PfPanK1 minus its parasite-specific inserts is predicted by homology modeling using the AMPPNP and pantothenate-bound human PanK3 structure (PDB ID 5KPR) as a template. PfPanK1 shares 28% sequence identity with human PanK3 over the protein parts that are modeled
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F247V
less than 50% of catalytic activity of wild type, feedback resistant
H177Q
less than 50% of catalytic activity of wild type, feedback resistant
L236F
-
temperature-sensitive mutant, inactive above 39°C
R106A
50% of catalytic activity of wild type, feedback resistant
R315C
-
temperature-sensitive mutant, inactive above 39°C
S176L
-
temperature-sensitive mutant, inactive above 39°C
A267F
catalytically inactive
A269F
catalytically inactive
A509V
-
naturally occurring mutation, early onset in patients, 105% activity compared to the wild-type enzyme
E134G
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G19V
site-directed mutagenesis, PANK3(G19V) cannot bind ATP, and biochemical analyses of an engineered PANK3/PANK3(G19V) heterodimer confirmed that the two active sites are functionally coupled. Analysis of PANK3/PANK3(G19V) heterodimers, overview
K224A
-
site-directed mutagenesis, less than 0.2% activity compared to the wild-type enzyme
N404I
-
naturally occurring mutation, early and late onset in patients, 83% activity compared to the wild-type enzyme
N500I
-
naturally occurring mutation, early onset in patients, 3.9% activity compared to the wild-type enzyme
R207A
catalytically inactive
R264W
-
naturally occurring mutation, early onset in patients, 58% activity compared to the wild-type enzyme
R286C
-
naturally occurring mutation, early and late onset in patients, 176% activity compared to the wild-type enzyme
R532W
-
naturally occurring mutation, early onset in patients, 95% activity compared to the wild-type enzyme
S195V
the mutant is insensitive to acetyl-CoA and has a KM defect for pantothenate
S351P
-
naturally occurring mutation, early and late onset in patients, 78% activity compared to the wild-type enzyme
S471N
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T327I
-
naturally occurring mutation, early onset in patients, 91% activity compared to the wild-type enzyme
F247A
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
F254A
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
F254A/F247A
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
F247A
-
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
-
F254A
-
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
-
F254A/F247A
-
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
-
F247A
-
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
-
F254A
-
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
-
F254A/F247A
-
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
-
D101A
reduced enzymatic activity
D121A
reduced enzymatic activity
H156A
slightly increased enzymatic activity
K13A
reduced enzymatic activity
N9G
strongly reduced enzymatic activity
T157A
reduced enzymatic activity
G351S
-
temperature-sensitive phenotype
D6A
reduced enzymatic activity
E70A
reduced enzymatic activity
K13A
reduced enzymatic activity
L11A
reduced enzymatic activity
L263P
reduced enzymatic activity
T10A
reduced enzymatic activity
Y137A
reduced enzymatic activity
D105E
-
less than 6% activity of the wild type enzyme
D105N
-
less than 6% activity of the wild type enzyme
D125E
-
less than 6% activity of the wild type enzyme
D125N
-
less than 6% activity of the wild type enzyme
D6E
-
less than 6% activity of the wild type enzyme
D6N
-
less than 6% activity of the wild type enzyme
E138V
site-directed mutagenesis, inactive mutant
E138V
naturally occuring mutation in isozyme PanK4, inactive mutant
G219V
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G219V
-
naturally occurring mutation, early and late onset in patients, 0.4% activity compared to the wild-type enzyme
G521R
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G521R
-
the splice variant PanK2 naturally contains mutation which is associated with neurodegenerative disease in brain, early and late onset in patients, less than 0.2% activity compared to the wild-type enzyme
G521R
loss of enzyme activity
R207W
site-directed mutagenesis, inactive mutant
R207W
naturally occuring mutation in isozyme PanK4, inactive mutant
T234A
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T234A
-
naturally occurring mutation, early and late onset in patients, 112% activity compared to the wild-type enzyme
T528M
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T528M
-
naturally occurring mutation, early and late onset in patients, 146% activity compared to the wild-type enzyme
T528M
no effect on PANK2 activity or stability
additional information
epigenetic gene silencing of PanK resulting in a significant reduction of PanK activity, intracellular CoA concentrations, and growth retardation in vitro, reinforcing the importance of this gene in Entamoeba histolytica. In Pank-silenced cells, the genes encoding other enzymes involved in CoA biosynthesis are upregulated 1.2, 2.1, 3.0, and 5.2 fold for PPCS-PPCDC, PPAT, DPCK1, and DPCK2, respectively. Growth kinetic analysis
additional information
-
epigenetic gene silencing of PanK resulting in a significant reduction of PanK activity, intracellular CoA concentrations, and growth retardation in vitro, reinforcing the importance of this gene in Entamoeba histolytica. In Pank-silenced cells, the genes encoding other enzymes involved in CoA biosynthesis are upregulated 1.2, 2.1, 3.0, and 5.2 fold for PPCS-PPCDC, PPAT, DPCK1, and DPCK2, respectively. Growth kinetic analysis
additional information
an allelic variant mislocates and thereby causes disease
additional information
-
an allelic variant mislocates and thereby causes disease
additional information
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identification of naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease, identification of other disease related point mutations which lead to reduced enzyme activity, mutations alter processing, stability, and catalytic activity of the mutant PanK2
additional information
-
several natural mutants with frame shifts show no activity, identification of mutants with mutations which introduce stop codons, overview
additional information
-
two siblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration have the I346S mutation in pantothenate kinase-2
additional information
-
human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity
additional information
human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity
additional information
-
construction of chimeric mutant enzymes PanK1beta-3-1beta and PanK3-1beta-3 by combination of isozymes PanK3 and PanK1beta, mutant show different sensitivity to feedback inhibitors compared to the wild-type isozymes, overview
additional information
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generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/- Pank-/-double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/- Pank-/-double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/- Pank-/-double knock-out mice
additional information
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generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/-Pank-/-3 double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/-Pank-/-3 double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/-Pank-/-3 double knock-out mice
additional information
generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
additional information
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generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
additional information
-
generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
-
additional information
-
generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
-
additional information
parasites pressured with pantothenol or CJ-15,801 become resistant to these antiplasmodial pantothenate analogues. Pfpank1 mutations mediate parasite resistance to PanOH and CJ-15,801. Whole-genome sequencing reveals mutations in one of two putative PanK genes (Pfpank1) in each resistant line. These mutations significantly alter PfPanK activity, with two conferring a fitness cost, consistent with Pfpank1 coding for a functional PanK that is essential for normal growth. Pfpank1 disruption plasmid, DELTAPfpank1-pCC-1 (SI), is transfected into wild-type Palsmodium falciparum strain 3D7
additional information
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parasites pressured with pantothenol or CJ-15,801 become resistant to these antiplasmodial pantothenate analogues. Pfpank1 mutations mediate parasite resistance to PanOH and CJ-15,801. Whole-genome sequencing reveals mutations in one of two putative PanK genes (Pfpank1) in each resistant line. These mutations significantly alter PfPanK activity, with two conferring a fitness cost, consistent with Pfpank1 coding for a functional PanK that is essential for normal growth. Pfpank1 disruption plasmid, DELTAPfpank1-pCC-1 (SI), is transfected into wild-type Palsmodium falciparum strain 3D7
additional information
expression of acetyl-CoA carboxylase (acc) obtained from Corynebacterium glutamicum in Escherichia coli, it causes accumulation of 2.2fold more fatty acids in Escherichia coli that in the wild-type. The addition of gene coaX encoding patothenate kinase from Pseudomonas putida or fatty acid synthase (fasA) from Corynebacterium glutamicum results in a 3.1 and 3.6fold increased fatty acid synthesis in Escherichia coli cells, which express acc and coaA, or acc and fasA, respectively. The transformants, simultaneously possessing all three genes, produce 5.6fold more fatty acids. The strain possessing acc, coaA, and fasA stores 691 mg/l of fatty acids, primarily as phospholipids, inside the inner membrane after 72-h cultivation. In addition, 19% of the total CoA pool is occupied by malonyl-CoA
additional information
improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
additional information
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improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
additional information
-
improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
-
additional information
-
improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
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Acta Crystallogr. Sect. D
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Escherichia coli (P0A6I3), Escherichia coli, Mycobacterium tuberculosis (P9WPA7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPA7)
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Escherichia coli, Mycobacterium tuberculosis (P9WPA7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPA7)
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2009
Saccharomyces cerevisiae
brenda
Wu, Z.; Li, C.; Lv, S.; Zhou, B.
Pantothenate kinase-associated neurodegeneration: insights from a Drosophila model
Hum. Mol. Genet.
18
3659-3672
2009
Drosophila melanogaster, Homo sapiens (Q9BZ23), Homo sapiens
brenda
Takagi, M.; Tamaki, H.; Miyamoto, Y.; Leonardi, R.; Hanada, S.; Jackowski, S.; Chohnan, S.
Pantothenate kinase from the thermoacidophilic archaeon Picrophilus torridus
J. Bacteriol.
192
233-241
2010
Picrophilus torridus (Q6L2I5), Picrophilus torridus
brenda
Doi, H.; Koyano, S.; Miyatake, S.; Matsumoto, N.; Kameda, T.; Tomita, A.; Miyaji, Y.; Suzuki, Y.; Sawaishi, Y.; Kuroiwa, Y.
Siblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration and a novel mutation, Ile346Ser, in PANK2: Clinical features and (99m)Tc-ECD brain perfusion SPECT findings
J. Neurol. Sci.
290
172-176
2009
Homo sapiens
brenda
Rowan, A.S.; Nicely, N.I.; Cochrane, N.; Wlassoff, W.A.; Claiborne, A.; Hamilton, C.J.
Nucleoside triphosphate mimicry: a sugar triazolyl nucleoside as an ATP-competitive inhibitor of B. anthracis pantothenate kinase
Org. Biomol. Chem.
7
4029-4036
2009
Bacillus anthracis
brenda
Chetnani, B.; Kumar, P.; Abhinav, K.V.; Chhibber, M.; Surolia, A.; Vijayan, M.
Location and conformation of pantothenate and its derivatives in Mycobacterium tuberculosis pantothenate kinase: insights into enzyme action
Acta Crystallogr. Sect. D
67
774-783
2011
Mycobacterium tuberculosis (P9WPA7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPA7)
brenda
Leonardi, R.; Zhang, Y.M.; Yun, M.K.; Zhou, R.; Zeng, F.Y.; Lin, W.; Cui, J.; Chen, T.; Rock, C.O.; White, S.W.; Jackowski, S.
Modulation of pantothenate kinase 3 activity by small molecules that interact with the substrate/allosteric regulatory domain
Chem. Biol.
17
892-902
2010
Homo sapiens, Homo sapiens (Q9H999)
brenda
Gutierrez, L.; Sabaratnam, N.; Aktar, R.; Bettedi, L.; Mandilaras, K.; Missirlis, F.
Zinc accumulation in heterozygous mutants of fumble, the pantothenate kinase homologue of Drosophila
FEBS Lett.
584
2942-2946
2010
Drosophila melanogaster
brenda
Venkatraman, J.; Bhat, J.; Solapure, S.M.; Sandesh, J.; Sarkar, D.; Aishwarya, S.; Mukherjee, K.; Datta, S.; Malolanarasimhan, K.; Bandodkar, B.; Das, K.S.
Screening, identification, and characterization of mechanistically diverse inhibitors of the Mycobacterium tuberculosis enzyme, pantothenate kinase (CoaA)
J. Biomol. Screen.
17
293-302
2012
Mycobacterium tuberculosis
brenda
Mandakh, A.; Niraula, N.P.; Kim, E.P.; Sohng, J.K.
Identification and characterization of a pantothenate kinase (PanK-sp) from Streptomyces peucetius ATCC 27952
J. Microbiol. Biotechnol.
20
1689-1695
2010
Streptomyces peucetius (D2K764), Streptomyces peucetius, Streptomyces peucetius ATCC 27952 (D2K764)
brenda
Chetnani, B.; Kumar, P.; Surolia, A.; Vijayan, M.
M. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations
J. Mol. Biol.
400
171-185
2010
Mycobacterium tuberculosis
brenda
Awasthy, D.; Ambady, A.; Bhat, J.; Sheikh, G.; Ravishankar, S.; Subbulakshmi, V.; Mukherjee, K.; Sambandamurthy, V.; Sharma, U.
Essentiality and functional analysis of type I and type III pantothenate kinases of Mycobacterium tuberculosis
Microbiology
156
2691-2701
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (ATCC 27294)
brenda
Leonardi, R.; Rehg, J.E.; Rock, C.O.; Jackowski, S.
Pantothenate kinase 1 is required to support the metabolic transition from the fed to the fasted state
PLoS ONE
5
e11107
2010
Mus musculus
brenda
Ishibashi, T.; Tomita, H.; Yokooji, Y.; Morikita, T.; Watanabe, B.; Hiratake, J.; Kishimoto, A.; Kita, A.; Miki, K.; Imanaka, T.; Atomi, H.
A detailed biochemical characterization of phosphopantothenate synthetase, a novel enzyme involved in coenzyme A biosynthesis in the Archaea
Extremophiles
16
819-828
2012
Thermococcus kodakarensis (Q5JHF1), Thermococcus kodakarensis
brenda
Awuah, E.; Ma, E.; Hoegl, A.; Vong, K.; Habib, E.; Auclair, K.
Exploring structural motifs necessary for substrate binding in the active site of Escherichia coli pantothenate kinase
Bioorg. Med. Chem.
22
3083-3090
2014
Escherichia coli (P0A6I3), Escherichia coli
brenda
Ogata, Y.; Katoh, H.; Asayama, M.; Chohnan, S.
Role of prokaryotic type I and III pantothenate kinases in the coenzyme A biosynthetic pathway of Bacillus subtilis
Can. J. Microbiol.
60
297-305
2014
Bacillus subtilis
brenda
Bjoerkelid, C.; Bergfors, T.; Raichurkar, A.K.; Mukherjee, K.; Malolanarasimhan, K.; Bandodkar, B.; Jones, T.A.
Structural and biochemical characterization of compounds inhibiting Mycobacterium tuberculosis pantothenate kinase
J. Biol. Chem.
288
18260-18270
2013
Mycobacterium tuberculosis (P9WPA7), Mycobacterium tuberculosis
brenda
Ogata, Y.; Chohnan, S.
Prokaryotic type III pantothenate kinase enhances coenzyme A biosynthesis in Escherichia coli
J. Gen. Appl. Microbiol.
61
266-269
2016
Escherichia coli
brenda
Li, B.; Tempel, W.; Smil, D.; Bolshan, Y.; Schapira, M.; Park, H.W.
Crystal structures of Klebsiella pneumoniae pantothenate kinase in complex with N-substituted pantothenamides
Proteins
81
1466-1472
2013
Klebsiella pneumoniae (B5XYG3), Klebsiella pneumoniae, Klebsiella pneumoniae 342 (B5XYG3)
brenda
Hughes, S.J.; Antoshchenko, T.; Kim, K.P.; Smil, D.; Park, H.W.
Structural characterization of a new N-substituted pantothenamide bound to pantothenate kinases from Klebsiella pneumoniae and Staphylococcus aureus
Proteins
82
1542-1548
2014
Klebsiella pneumoniae (B5XYG3), Klebsiella pneumoniae, Staphylococcus aureus (Q6G7I0), Staphylococcus aureus, Staphylococcus aureus MSSA476 (Q6G7I0), Klebsiella pneumoniae 342 (B5XYG3)
brenda
Hughes, S.J.; Barnard, L.; Mottaghi, K.; Tempel, W.; Antoshchenko, T.; Hong, B.S.; Allali-Hassani, A.; Smil, D.; Vedadi, M.; Strauss, E.; Park, H.W.
Discovery of potent pantothenamide inhibitors of Staphylococcus aureus pantothenate kinase through a minimal SAR study inhibition is due to trapping of the product
ACS Infect. Dis.
2
627-641
2016
Staphylococcus aureus (A0A167Z3Z6), Staphylococcus aureus, Staphylococcus aureus RN4220 (A0A167Z3Z6)
brenda
Paul, A.; Kumar, P.; Surolia, A.; Vijayan, M.
Biochemical and structural studies of mutants indicate concerted movement of the dimer interface and ligand-binding region of Mycobacterium tuberculosis pantothenate kinase
Acta Crystallogr. Sect. F
73
635-643
2017
Mycobacterium tuberculosis (P9WPA1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPA1), Mycobacterium tuberculosis ATCC 25618 (P9WPA1)
brenda
Liu, W.; Zhang, B.; Jiang, R.
Improving acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass
Biotechnol. Biofuels
10
41
2017
Saccharomyces cerevisiae (Q04430), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742 (Q04430), Saccharomyces cerevisiae ATCC 204508 (Q04430)
brenda
Satoh, S.; Ozaki, M.; Matsumoto, S.; Nabatame, T.; Kaku, M.; Shudo, T.; Asayama, M.; Chohnan, S.
Enhancement of fatty acid biosynthesis by exogenous acetyl-CoA carboxylase and pantothenate kinase in Escherichia coli
Biotechnol. Lett.
42
2595-2605
2020
Pseudomonas putida (V5XWU6)
brenda
Spry, C.; Sewell, A.L.; Hering, Y.; Villa, M.V.J.; Weber, J.; Hobson, S.J.; Harnor, S.J.; Gul, S.; Marquez, R.; Saliba, K.J.
Structure-activity analysis of CJ-15,801 analogues that interact with Plasmodium falciparum pantothenate kinase and inhibit parasite proliferation
Eur. J. Med. Chem.
143
1139-1147
2018
Plasmodium falciparum (Q8ILP4), Plasmodium falciparum
brenda
Nurkanto, A.; Jeelani, G.; Yamamoto, T.; Naito, Y.; Hishiki, T.; Mori, M.; Suematsu, M.; Shiomi, K.; Hashimoto, T.; Nozaki, T.
Characterization and validation of Entamoeba histolytica pantothenate kinase as a novel anti-amebic drug target
Int. J. Parasitol. Drugs Drug Resist.
8
125-136
2018
Entamoeba histolytica (B1N2P3), Entamoeba histolytica
brenda
Subramanian, C.; Yun, M.K.; Yao, J.; Sharma, L.K.; Lee, R.E.; White, S.W.; Jackowski, S.; Rock, C.O.
Allosteric regulation of mammalian pantothenate kinase
J. Biol. Chem.
291
22302-22314
2016
Mus musculus, Mus musculus (Q8K4K6), Mus musculus (Q8R2W9), Homo sapiens (Q8TE04), Homo sapiens (Q9BZ23), Homo sapiens (Q9H999), Homo sapiens
brenda
Chiu, J.E.; Thekkiniath, J.; Mehta, S.; Mueller, C.; Bracher, F.; Ben Mamoun, C.
The yeast pantothenate kinase Cab1 is a master regulator of sterol metabolism and of susceptibility to ergosterol biosynthesis inhibitors
J. Biol. Chem.
294
14757-14767
2019
Saccharomyces cerevisiae (Q04430), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q04430)
brenda
Tjhin, E.T.; Spry, C.; Sewell, A.L.; Hoegl, A.; Barnard, L.; Sexton, A.E.; Siddiqui, G.; Howieson, V.M.; Maier, A.G.; Creek, D.J.; Strauss, E.; Marquez, R.; Auclair, K.; Saliba, K.J.
Mutations in the pantothenate kinase of Plasmodium falciparum confer diverse sensitivity profiles to antiplasmodial pantothenate analogues
PLoS Pathog.
14
e1006918
2018
Plasmodium falciparum (Q8ILP4), Plasmodium falciparum
brenda
Yao, J.; Subramanian, C.; Rock, C.O.; Jackowski, S.
Human pantothenate kinase 4 is a pseudo-pantothenate kinase
Protein Sci.
28
1031-1047
2019
Homo sapiens, Homo sapiens (Q9H999)
brenda