Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 3'-dephospho-CoA
ADP + CoA
ATP + dephospho-CoA
ADP + CoA
ATP + dephospho-tryptamine-CoA
ADP + tryptamine-CoA
-
-
-
-
?
CTP + 3'-dephospho-CoA
CDP + CoA
GTP + 3'-dephospho-CoA
GDP + CoA
TTP + 3'-dephospho-CoA
TDP + CoA
UTP + 3'-dephospho-CoA
UDP + CoA
additional information
?
-
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
low activity
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
low activity
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
low activity
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
specific
-
?
ATP + dephospho-CoA
ADP + CoA
-
ITP or ADP are no substrates
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
specific
-
?
ATP + dephospho-CoA
ADP + CoA
-
ITP or ADP are no substrates
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
ir
ATP + dephospho-CoA
ADP + CoA
-
last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
ir
ATP + dephospho-CoA
ADP + CoA
-
final step of coenzyme A biosynthesis
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
ir
ATP + dephospho-CoA
ADP + CoA
-
specific
-
?
ATP + dephospho-CoA
ADP + CoA
-
no substrates are 3'-dephospho-alpha-carboxy-CoA
-
?
ATP + dephospho-CoA
ADP + CoA
-
involved in coenzyme A biosynthesis, last irreversible reaction
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
final step of coenzyme A biosynhesis
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
-
final step of coenzyme A biosynhesis
-
-
?
CTP + 3'-dephospho-CoA
CDP + CoA
15.4% activity compared to ATP
-
-
?
CTP + 3'-dephospho-CoA
CDP + CoA
7.3% activity compared to ATP
-
-
?
GTP + 3'-dephospho-CoA
GDP + CoA
32.6% activity compared to ATP
-
-
?
GTP + 3'-dephospho-CoA
GDP + CoA
33% activity compared to ATP
-
-
?
GTP + 3'-dephospho-CoA
GDP + CoA
gene TK1697 encodes a GTP-dependent dephospho-CoA kinase
-
-
?
GTP + 3'-dephospho-CoA
GDP + CoA
gene TK1697 encodes a GTP-dependent dephospho-CoA kinase
-
-
?
GTP + 3'-dephospho-CoA
GDP + CoA
gene TK1697 encodes a GTP-dependent dephospho-CoA kinase
-
-
?
TTP + 3'-dephospho-CoA
TDP + CoA
24.1% activity compared to ATP
-
-
?
TTP + 3'-dephospho-CoA
TDP + CoA
4.9% activity compared to ATP
-
-
?
UTP + 3'-dephospho-CoA
UDP + CoA
2.6% activity compared to ATP
-
-
?
UTP + 3'-dephospho-CoA
UDP + CoA
4.5% activity compared to ATP
-
-
?
additional information
?
-
-
assay method: arsenolysis of dephospho-CoA, formation of CoA
-
-
?
additional information
?
-
-
assay method: arsenolysis of dephospho-CoA, formation of CoA
-
-
?
additional information
?
-
pantothenate is no substrate
-
-
-
additional information
?
-
pantothenate is no substrate
-
-
-
additional information
?
-
-
pantothenate is no substrate
-
-
-
additional information
?
-
when NADx02, ADP, AMP, adenosine, or ribose are substituted for dephospho-CoA as phosphate acceptors, no detectable amount of GDP is produced, indicating specificity of the TK1697 protein toward dephospho-CoA. GTP is the preferred phosphate donor
-
-
-
additional information
?
-
-
when NADx02, ADP, AMP, adenosine, or ribose are substituted for dephospho-CoA as phosphate acceptors, no detectable amount of GDP is produced, indicating specificity of the TK1697 protein toward dephospho-CoA. GTP is the preferred phosphate donor
-
-
-
additional information
?
-
when NADx02, ADP, AMP, adenosine, or ribose are substituted for dephospho-CoA as phosphate acceptors, no detectable amount of GDP is produced, indicating specificity of the TK1697 protein toward dephospho-CoA. GTP is the preferred phosphate donor
-
-
-
additional information
?
-
when NADx02, ADP, AMP, adenosine, or ribose are substituted for dephospho-CoA as phosphate acceptors, no detectable amount of GDP is produced, indicating specificity of the TK1697 protein toward dephospho-CoA. GTP is the preferred phosphate donor
-
-
-
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0217 - 0.501
3'-dephospho-CoA
0.003 - 0.76
dephospho-CoA
0.26
GTP
pH 8.0, 80°C, recombinant enzyme
additional information
additional information
-
0.0217
3'-dephospho-CoA
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0349
3'-dephospho-CoA
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0372
3'-dephospho-CoA
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0579
3'-dephospho-CoA
pH 8.0, 37°C, isozyme Ehdpck2
0.0758
3'-dephospho-CoA
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0809
3'-dephospho-CoA
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0877
3'-dephospho-CoA
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.114
3'-dephospho-CoA
pH 8.0, 37°C, isozyme Ehdpck1
0.14
3'-dephospho-CoA
pH 8.0, 80°C, recombinant enzyme
0.181
3'-dephospho-CoA
mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.501
3'-dephospho-CoA
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.015
ATP
pH 8.0, 37°C, isozyme Ehdpck2
0.0196
ATP
pH 8.0, 37°C, isozyme Ehdpck1
0.0345
ATP
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0501
ATP
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0568
ATP
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0575
ATP
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0598
ATP
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0639
ATP
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0867
ATP
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.1
ATP
-
cytosolic enzyme
0.14
ATP
-
native wild-type enzyme, pH 8.5, 25°C
0.19
ATP
recombinant enzyme, pH 8.0, 25°C
0.33
ATP
recombinant enzyme, pH 8.0, 25°C
0.003
dephospho-CoA
-
pH 8.2, 37°C
0.0041
dephospho-CoA
native enzyme, pH 8.0, 25°C
0.0052
dephospho-CoA
recombinant enzyme, pH 8.0, 25°C
0.01
dephospho-CoA
-
mitochondrial enzyme
0.76
dephospho-CoA
-
native wild-type enzyme, pH 8.5, 25°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
both ATP and dephospho-CoA exhibit hyperbolic saturation kinetics when assayed over the range of 0.004-0.128 mM dephospho-CoA in the presence of 0.10 mM ATP and in the range of 0.001-0.10 mM ATP substrate in the presence of 0.128 mM dephospho-CoA
-
additional information
additional information
both ATP and dephospho-CoA exhibit hyperbolic saturation kinetics when assayed over the range of 0.004-0.128 mM dephospho-CoA in the presence of 0.10 mM ATP and in the range of 0.001-0.10 mM ATP substrate in the presence of 0.128 mM dephospho-CoA
-
additional information
additional information
-
both ATP and dephospho-CoA exhibit hyperbolic saturation kinetics when assayed over the range of 0.004-0.128 mM dephospho-CoA in the presence of 0.10 mM ATP and in the range of 0.001-0.10 mM ATP substrate in the presence of 0.128 mM dephospho-CoA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0017 - 5.57
3'-dephospho-CoA
6.68
GTP
pH 8.0, 80°C, recombinant enzyme
0.0017
3'-dephospho-CoA
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0076
3'-dephospho-CoA
mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0255
3'-dephospho-CoA
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0257
3'-dephospho-CoA
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0293
3'-dephospho-CoA
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0327
3'-dephospho-CoA
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0334
3'-dephospho-CoA
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0569
3'-dephospho-CoA
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.96
3'-dephospho-CoA
pH 8.0, 37°C, isozyme Ehdpck2
1.48
3'-dephospho-CoA
pH 8.0, 37°C, isozyme Ehdpck1
5.57
3'-dephospho-CoA
pH 8.0, 80°C, recombinant enzyme
0.014
ATP
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0192
ATP
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.039
ATP
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.043
ATP
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0481
ATP
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0651
ATP
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.067
ATP
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
1.05
ATP
pH 8.0, 37°C, isozyme Ehddpck2
1.41
ATP
pH 8.0, 37°C, isozyme Ehdpck1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00034 - 39.79
3'-dephospho-CoA
25.69
GTP
pH 8.0, 80°C, recombinant enzyme
0.00034
3'-dephospho-CoA
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.0015
3'-dephospho-CoA
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.042
3'-dephospho-CoA
mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.337
3'-dephospho-CoA
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.38
3'-dephospho-CoA
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.69
3'-dephospho-CoA
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.703
3'-dephospho-CoA
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.838
3'-dephospho-CoA
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
12.98
3'-dephospho-CoA
pH 8.0, 37°C, isozyme Ehdpck1
16.58
3'-dephospho-CoA
pH 8.0, 37°C, isozyme Ehdpck2
39.79
3'-dephospho-CoA
pH 8.0, 80°C, recombinant enzyme
0.243
ATP
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.3
ATP
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.448
ATP
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.713
ATP
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
0.847
ATP
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
1.3
ATP
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
1.93
ATP
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C
70
ATP
pH 8.0, 37°C, isozyme Ehdpck2
71.43
ATP
pH 8.0, 37°C, isozyme Ehdpck1
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.
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.
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.
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.
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.
evolution
all the eukaryotic-type enzymes of CoA de novo biosynthesis pathway are conserved in all Plasmodium species. Unlike mammalian cells and similar to bacteria, the PPAT and DPCK enzymes are encoded on two different genes and not on one gene that encodes a bifunctional protein
evolution
enzyme DPCK, encoded by the TK1697 gene of Thermococcus kodakarensis is not homologous to the classical DPCK from bacteria and eukaryotes but is distantly related to bacterial and eukaryotic thiamine diphosphokinases. Orthologues of TK1697 are widely distributed in archaea, suggesting that this form of DPCK is responsible for the last step of CoA biosynthesis in most of the archaea
evolution
-
enzyme DPCK, encoded by the TK1697 gene of Thermococcus kodakarensis is not homologous to the classical DPCK from bacteria and eukaryotes but is distantly related to bacterial and eukaryotic thiamine diphosphokinases. Orthologues of TK1697 are widely distributed in archaea, suggesting that this form of DPCK is responsible for the last step of CoA biosynthesis in most of the archaea
-
evolution
-
enzyme DPCK, encoded by the TK1697 gene of Thermococcus kodakarensis is not homologous to the classical DPCK from bacteria and eukaryotes but is distantly related to bacterial and eukaryotic thiamine diphosphokinases. Orthologues of TK1697 are widely distributed in archaea, suggesting that this form of DPCK is responsible for the last step of CoA biosynthesis in most of the archaea
-
malfunction
disruption of the TK1697 results in CoA auxotrophy
malfunction
-
disruption of the TK1697 results in CoA auxotrophy
-
malfunction
-
disruption of the TK1697 results in CoA auxotrophy
-
metabolism
conservation of CoA biosynthesis pathway in all malaria parasite species. A schematic representation of the canonical biosynthesis pathway of CoA from pantothenate with enzymes PanK (pantothenate kinase), PPCS (phosphopantothenylcysteine synthase), PPCDC (phosphopantothenylcysteine decarboxylase), PPAT (phosphopantetheine adenylyltransferase), and DPCK (dephospho-CoA kinase), respectively. In contrast to the first two enzymes of this pathway, the last two enzymes for CoA biosynthesis are essential for blood stage parasites
metabolism
the enzyme DCPK catalyzes the final step in the biosynthesis of CoA
metabolism
the pathway for CoA biosynthesis in archaea compared to those of plants and bacteria, overview
metabolism
-
the pathway for CoA biosynthesis in archaea compared to those of plants and bacteria, overview
-
metabolism
-
the pathway for CoA biosynthesis in archaea compared to those of plants and bacteria, overview
-
physiological function
in the cytosol, the monofunctional DPCK transforms dephospho-CoA to CoA
physiological function
the enzyme is involved in biosynthesis of CoA, an essential cofactor for all prokaryotes and eukaryotes to support a large number of metabolic processes including fatty acid biosynthesis and oxidation, as well as carbohydrate and amino acid metabolism. PPAT (phosphopantetheine adenylyltransferase), and DPCK (dephospho-CoA kinase) are essential for growth of blood stage parasites
physiological function
TK1697 gene-encoded DPCK contributes to CoA biosynthesis in Thermococcus kodakarensis. CoA is utilized in a wide range of metabolic pathways, and its biosynthesis is essential for life
physiological function
-
TK1697 gene-encoded DPCK contributes to CoA biosynthesis in Thermococcus kodakarensis. CoA is utilized in a wide range of metabolic pathways, and its biosynthesis is essential for life
-
physiological function
-
TK1697 gene-encoded DPCK contributes to CoA biosynthesis in Thermococcus kodakarensis. CoA is utilized in a wide range of metabolic pathways, and its biosynthesis is essential for life
-
additional information
intracellular metabolite extraction of wild-type expressing and silenced-mutant strain. DPCKs comprise three domains: the nucleotide-binding domain in parallel beta-sheet, the substrate-binding domain in alpha-helices, and the LID domain. All of these DPCK features are present in EhDPCK. Isozymes EhDPCK1 and 2 show striking similarity based on three-dimensional structure predicted by homology modeling, structural comparison of EhDPCK and its mammalian counterpart from mouse, overview
additional information
intracellular metabolite extraction of wild-type expressing and silenced-mutant strain. DPCKs comprise three domains: the nucleotide-binding domain in parallel beta-sheet, the substrate-binding domain in alpha-helices, and the LID domain. All of these DPCK features are present in EhDPCK. Isozymes EhDPCK1 and 2 show striking similarity based on three-dimensional structure predicted by homology modeling, structural comparison of EhDPCK and its mammalian counterpart from mouse, overview
additional information
-
intracellular metabolite extraction of wild-type expressing and silenced-mutant strain. DPCKs comprise three domains: the nucleotide-binding domain in parallel beta-sheet, the substrate-binding domain in alpha-helices, and the LID domain. All of these DPCK features are present in EhDPCK. Isozymes EhDPCK1 and 2 show striking similarity based on three-dimensional structure predicted by homology modeling, structural comparison of EhDPCK and its mammalian counterpart from mouse, overview
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D32A
the mutant shows a catalytic efficiency of only 5% of the native enzyme
D32E
the mutant shows increased catalytic efficiency compared to the wild type enzyme
D32N
the mutant shows an almost 2.54times increased Km value for 3'-dephospho-CoA compared to the wild type enzyme. The absence of magnesium completely ablates activity for the D32N mutant
G8A
this mutation does not change either the Km or the Kcat of the reaction considerably
K14A
the substitution affects the kinetic parameters of the reaction resulting in a mere 19% reduction in the Kcat of the enzyme, the mutant demonstrates a 50% increase in the Km for ATP
L114A
the mutation results in a decrease in the affinity of the enzyme for the acceptor substrate
R140A
this mutation completely abolishes kinetic activity
R140K
the mutation results in a dramatic loss of catalytic activity
additional information
generation of trophozoites of Ehdpck1 and Ehdpck2 gene-silenced strains. Ehdpck1 and Ehdpck2 gene-silenced strains show significant growth defect in normal growth medium. The level of growth inhibition by Ehdpck2 gene silencing is more severe compared to that by Ehdpck1 gene silencing
additional information
generation of trophozoites of Ehdpck1 and Ehdpck2 gene-silenced strains. Ehdpck1 and Ehdpck2 gene-silenced strains show significant growth defect in normal growth medium. The level of growth inhibition by Ehdpck2 gene silencing is more severe compared to that by Ehdpck1 gene silencing
additional information
-
generation of trophozoites of Ehdpck1 and Ehdpck2 gene-silenced strains. Ehdpck1 and Ehdpck2 gene-silenced strains show significant growth defect in normal growth medium. The level of growth inhibition by Ehdpck2 gene silencing is more severe compared to that by Ehdpck1 gene silencing
additional information
experiments to generate a single gene deletion of DPCK in Plasmodium yoelii 17X-NL parasites show that the inability to delete PyPPAT and PyDPCK is not due to a technical reason, nor the inability to access the gene loci, but due to a crucial role that both enzymes play in the growth and/or survival of blood stage parasites in mouse erythrocytes
additional information
-
experiments to generate a single gene deletion of DPCK in Plasmodium yoelii 17X-NL parasites show that the inability to delete PyPPAT and PyDPCK is not due to a technical reason, nor the inability to access the gene loci, but due to a crucial role that both enzymes play in the growth and/or survival of blood stage parasites in mouse erythrocytes
additional information
disruption of the TK1697 resulting in CoA auxotrophy. The DELTATK1697 mutant is inoculated in ASW-YT-pyruvate-agmatine medium, but no growth is observed. When 1 mM CoA is added to the medium, the growth defect is partially complemented, with lower growth rate and less cell yield than the wild-type strain KPD1. In the strain transformed with pRPETK1697, the growth defect is almost fully complemented
additional information
-
disruption of the TK1697 resulting in CoA auxotrophy. The DELTATK1697 mutant is inoculated in ASW-YT-pyruvate-agmatine medium, but no growth is observed. When 1 mM CoA is added to the medium, the growth defect is partially complemented, with lower growth rate and less cell yield than the wild-type strain KPD1. In the strain transformed with pRPETK1697, the growth defect is almost fully complemented
additional information
-
disruption of the TK1697 resulting in CoA auxotrophy. The DELTATK1697 mutant is inoculated in ASW-YT-pyruvate-agmatine medium, but no growth is observed. When 1 mM CoA is added to the medium, the growth defect is partially complemented, with lower growth rate and less cell yield than the wild-type strain KPD1. In the strain transformed with pRPETK1697, the growth defect is almost fully complemented
-
additional information
-
disruption of the TK1697 resulting in CoA auxotrophy. The DELTATK1697 mutant is inoculated in ASW-YT-pyruvate-agmatine medium, but no growth is observed. When 1 mM CoA is added to the medium, the growth defect is partially complemented, with lower growth rate and less cell yield than the wild-type strain KPD1. In the strain transformed with pRPETK1697, the growth defect is almost fully complemented
-
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.
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.
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.
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.
Brohn, F.H.; Trager, W.
Coenzyme A requirement of malaria parasites: enzymes of coenzyme A biosynthesis in normal duck erythrocytes and erythrocytes infected with Plasmodium lophurae
Proc. Natl. Acad. Sci. USA
72
2456-2458
1975
Anas platyrhynchos, no activity in Plasmodium lophurae
brenda
Nishimura, N.; Kakimoto, T.; Chibata, I.
Mechanism of coenzyme A biosynthesis by Sarcina lutea
J. Ferment. Technol.
61
95-99
1983
Micrococcus luteus
-
brenda
Hoagland, M.B.; Novelli, G.D.
Biosynthesis of coenzyme A from phosphopantetheine from pantothenate
J. Biol. Chem.
207
767-773
1954
Columba sp., Rattus norvegicus, Sus scrofa
brenda
Novelli, G.D.
Enzymatic synthesis and structure of CoA
Fed. Proc.
12
675-681
1953
Columba sp., Rattus norvegicus, Sus scrofa
brenda
Abiko, Y.
Pantothenic acid and coenzyme A: dephospho-CoA pyrophosphorylase and dephospho-CoA kinase as a possible bifunctional enzyme complex (ATP: pantetheine-4'-phosphate adenylyltransferase, ec 2.7.7.3 and ATP: dehospho-CoA 3'phosphotransferase, ec 2.7.1.24)
Methods Enzymol.
18A
358-364
1970
Rattus norvegicus
-
brenda
Worrall, D.M.; Tubbs, P.K.
A bifunctional enzyme complex in coenzyme A biosynthesis: purification of pantetheine phosphate adenylyltransferase and dephospho-CoA kinase
Biochem. J.
215
153-157
1983
Sus scrofa
brenda
Worrall, D.M.; Lambert, S.F.; Tubbs, P.K.
Limited proteolysis of pig liver CoA synthase: evidence for subunit identity
FEBS Lett.
187
277-279
1985
Sus scrofa
brenda
Skrede, S.; Halvorsen, O.
Mitochondrial biosynthesis of coenzyme A
Biochem. Biophys. Res. Commun.
91
1536-1542
1979
Rattus norvegicus
brenda
Skrede, S.; Halvorsen, O.
Mitochondrial pantetheinephosphate adenylyltransferase and dephospho-CoA kinase
Eur. J. Biochem.
131
57-63
1983
Rattus norvegicus
brenda
Martin, D.P.; Drueckhammer, D.G.
Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase
Biochem. Biophys. Res. Commun.
192
1155-1161
1993
Corynebacterium ammoniagenes
brenda
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
Wang, T.P.; Kaplan, N.O.
Kinases for the synthesis of coenzyme A and triphosphopyridine nucleotide
J. Biol. Chem.
206
311-325
1954
Anas platyrhynchos, Columba sp.
brenda
Mishra, P.; Park, P.K.; Drueckhammer, D.G.
Identification of yacE (coaE) as the structural gene for dephosphocoenzyme A kinase in Escherichia coli K-12
J. Bacteriol.
183
2774-2778
2001
Corynebacterium ammoniagenes, Escherichia coli (P0A6I9), Escherichia coli
brenda
O'Toole, N.; Barbosa, J.A.; Li, Y.; Hung, L.W.; Matte, A.; Cygler, M.
Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli
Protein Sci.
12
327-336
2003
Escherichia coli
brenda
Obmolova, G.; Teplyakov, A.; Bonander, N.; Eisenstein, E.; Howard, A.J.; Gilliland, G.L.
Crystal structure of dephospho-coenzyme A kinase from Haemophilus influenzae
J. Struct. Biol.
136
119-125
2001
Haemophilus influenzae (P44920), Haemophilus influenzae
brenda
Seto, A.; Murayama, K.; Toyama, M.; Ebihara, A.; Nakagawa, N.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8
Proteins
58
235-242
2005
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Wadler, C.; Cronan, J.E.
Dephospho-CoA kinase provides a rapid and sensitive radiochemical assay for coenzyme A and its thioesters
Anal. Biochem.
368
17-23
2007
Aquifex aeolicus, Escherichia coli, Homo sapiens
brenda
Hwang, Y.; Ganguly, S.; Ho, A.K.; Klein, D.C.; Cole, P.A.
Enzymatic and cellular study of a serotonin N-acetyltransferase phosphopantetheine-based prodrug
Bioorg. Med. Chem.
15
2147-2155
2007
Homo sapiens
brenda
Gudkova, D.; Panasyuk, G.; Nemazanyy, I.; Zhyvoloup, A.; Monteil, P.; Filonenko, V.; Gout, I.
EDC4 interacts with and regulates the dephospho-CoA kinase activity of CoA synthase
FEBS Lett.
586
3590-3595
2012
Homo sapiens
brenda
Walia, G.; Gajendar, K.; Surolia, A.
Identification of critical residues of the mycobacterial dephosphocoenzyme A kinase by site-directed mutagenesis
PLoS ONE
6
e15228
2011
Mycobacterium tuberculosis (P9WPA3)
brenda
Walia, G.; Surolia, A.
Insights into the regulatory characteristics of the mycobacterial dephosphocoenzyme A kinase: implications for the universal CoA biosynthesis pathway
PLoS ONE
6
e21390
2011
Mycobacterium tuberculosis
brenda
Yu, D.; Chen, X.; Xu, Z.; Ge, H.
Crystallization and preliminary X-ray characterization of the dephospho-CoA kinase from Legionella pneumophila
Acta Crystallogr. Sect. F
70
608-610
2014
Legionella pneumophila (Q5ZVH3), Legionella pneumophila
brenda
Lee, N.R.; Rimal, H.; Lee, J.H.; Oh, T.J.
Characterization of dephosphocoenzyme A kinase from Streptomyces peucetius ATCC27952, and its application for doxorubicin overproduction
J. Microbiol. Biotechnol.
24
1238-1244
2014
Streptomyces peucetius (D5MBE3), Streptomyces peucetius, Streptomyces peucetius ATCC 27952 (D5MBE3)
brenda
Gong, X.; Chen, X.; Yu, D.; Zhang, N.; Zhu, Z.; Niu, L.; Mao, Y.; Ge, H.
Crystal structure of Legionella pneumophila dephospho-CoA kinase reveals a non-canonical conformation of P-loop
J. Struct. Biol.
188
233-239
2014
Legionella pneumophila (Q5ZVH3), Legionella pneumophila
brenda
Vozza, A.; De Leonardis, F.; Paradies, E.; De Grassi, A.; Pierri, C.; Parisi, G.; Marobbio, C.; Lasorsa, F.; Muto, L.; Capobianco, L.; Dolce, V.; Raho, S.; Fiermonte, G.
Biochemical characterization of a new mitochondrial transporter of dephosphocoenzyme A in Drosophila melanogaster
Biochim. Biophys. Acta
1858
137-146
2017
Drosophila melanogaster (Q9VI57), Drosophila melanogaster
brenda
Hart, R.J.; Abraham, A.; Aly, A.S.I.
Genetic characterization of coenzyme A biosynthesis reveals essential distinctive functions during malaria parasite development in blood and mosquito
Front. Cell. Infect. Microbiol.
7
260
2017
Plasmodium yoelii (A0A077Y9A9), Plasmodium yoelii
brenda
Nurkanto, A.; Jeelani, G.; Yamamoto, T.; Hishiki, T.; Naito, Y.; Suematsu, M.; Hashimoto, T.; Nozaki, T.
Biochemical, metabolomic, and genetic analyses of dephospho coenzyme A kinase involved in coenzyme A biosynthesis in the human enteric parasite Entamoeba histolytica
Front. Microbiol.
9
2902
2018
Entamoeba histolytica (C4LWC7), Entamoeba histolytica (C4MB67), Entamoeba histolytica
brenda
Shimosaka, T.; Makarova, K.S.; Koonin, E.V.; Atomi, H.
Identification of dephospho-coenzyme A (dephospho-CoA) kinase in Thermococcus kodakarensis and elucidation of the entire CoA biosynthesis pathway in Archaea
mBio
10
e01146-19
2019
Thermococcus kodakarensis (Q5JIY7), Thermococcus kodakarensis, Thermococcus kodakarensis JCM 12380 (Q5JIY7), Thermococcus kodakarensis ATCC BAA-918 (Q5JIY7)
brenda