We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.
The taxonomic range for the selected organisms is: Homo sapiens The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphopantetheine adenylyltransferase, 4'-phosphopantetheine adenylyltransferase, pantetheine phosphate adenylyltransferase, pantetheine-phosphate adenylyltransferase, dephospho-coa pyrophosphorylase, enterococcus faecalis ppat,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3'-dephospho-CoA pyrophosphorylase
-
-
-
-
4-phosphopantetheine adenylyltransferase
-
dephospho-CoA pyrophosphorylase
-
-
-
-
dephospho-coenzyme A pyrophosphorylase
-
-
-
-
pantetheine phosphate adenylyltransferase
-
-
-
-
PPAT
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
nucleotidyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP:pantetheine-4'-phosphate adenylyltransferase
The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
-
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
slight inhibition in vivo
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
-
additional information
compound library screening, the series of reversible inhibitors show inhibition of cell growth of Gram-positive species but no or only slight inhibition of the human A-549 tumor cells, MIC values, overview. levels of inhibitory activity of compounds against Homo sapiens PPAT are measured in the forward direction. Only compound C shows poor inhibition in vivo
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cross Infection
Umbrella Sampling and X-ray Crystallographic Analysis Unveil an Arg-Asp Gate Facilitating Inhibitor Binding Inside Phosphopantetheine Adenylyltransferase Allosteric Cleft.
Pulmonary Disease, Chronic Obstructive
Rapid countermeasure discovery against Francisella tularensis based on a metabolic network reconstruction.
Respiratory Insufficiency
Umbrella Sampling and X-ray Crystallographic Analysis Unveil an Arg-Asp Gate Facilitating Inhibitor Binding Inside Phosphopantetheine Adenylyltransferase Allosteric Cleft.
Tuberculosis
Design of Novel Phosphopantetheine Adenylyltransferase Inhibitors: a Potential New Approach to Tackle Mycobacterium tuberculosis.
Tuberculosis
Kinetic, Thermodynamic, and Structural Insight into the Mechanism of Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis.
Tuberculosis
Rhombohedral crystals of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Tuberculosis
Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation.
Tuberculosis
Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Tuberculosis
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.005
(1S,2S)-N-(3,4-dichlorobenzyl)-2-(4,6-dimethoxypyrimidin-2-yl)cyclohexanecarboxamide
Homo sapiens
pH 7.0, 22°C, recombinant enzyme
0.024
2'-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6'-ethyl-4-hydroxy-6-oxo-1,6-dihydro-2,4'-bipyrimidine-5-carboxamide
Homo sapiens
pH 7.0, 22°C, recombinant enzyme
0.2
3-[3-(2-[(1S,2S)-2-[(3,4-dichlorobenzyl)carbamoyl]cyclohexyl]-6-ethylpyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]propanoic acid
Homo sapiens
pH 7.0, 22°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
22
assay at room temperature
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COASY_HUMAN
564
0
62329
Swiss-Prot
Secretory Pathway (Reliability: 5 )
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
recombinant enzyme PPAT from Escherichia coli strain BL21(DE3) to over 95% purity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli BL21
gene coaD, recombinant expression in Escherichia coli strain BL21(DE3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Aghajanian, S.; Worrall, D.M.
Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase)
Biochem. J.
365
13-18
2002
Homo sapiens (Q13057), Homo sapiens, Sus scrofa (Q8MIR4), Sus scrofa
brenda
de Jonge, B.L.; Walkup, G.K.; Lahiri, S.D.; Huynh, H.; Neckermann, G.; Utley, L.; Nash, T.J.; Brock, J.; San Martin, M.; Kutschke, A.; Johnstone, M.; Laganas, V.; Hajec, L.; Gu, R.F.; Ni, H.; Chen, B.; Hutchings, K.; Holt, E.; McKinney, D.; Gao, N.; Livchak, S.; Thresher, J.
Discovery of inhibitors of 4-phosphopantetheine adenylyltransferase (PPAT) to validate PPAT as a target for antibacterial therapy
Antimicrob. Agents Chemother.
57
6005-6015
2013
Candida albicans (B9WCR8), Enterococcus faecium, Enterococcus faecium ARC521, Escherichia coli (P0A6I6), Haemophilus influenzae (P44805), Haemophilus influenzae KW20 (P44805), Homo sapiens (Q06203), Staphylococcus aureus, Staphylococcus aureus RN4220, Streptococcus mutans (Q8DVH2), Streptococcus mutans UA159 (Q8DVH2), Streptococcus pneumoniae (Q8DNE6), Streptococcus pyogenes, Streptococcus pyogenes ARC838
brenda