2.7.1.24: dephospho-CoA kinase
This is an abbreviated version!
For detailed information about dephospho-CoA kinase, go to the full flat file.
Word Map on EC 2.7.1.24
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2.7.1.24
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adenylyltransferase
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phosphopantetheine
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pantothen
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4'-phosphopantetheine
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codhs
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copan
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analysis
- 2.7.1.24
- adenylyltransferase
- phosphopantetheine
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pantothen
- 4'-phosphopantetheine
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codhs
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copan
- analysis
Reaction
Synonyms
3'-dephospho-CoA kinase, CoaE, coenzyme A synthase, cytosolic monofunctional DPCK, dephospho coenzyme A kinase, dephospho-CoA kinase, dephospho-coenzyme A kinase, dephosphocoenzyme A, dephosphocoenzyme A kinase, dephosphocoenzyme A kinase (phosphorylating), DPCK, Dpck1, Dpck2, EhDPCK1, EhDPCK2, GTP-dependent dephospho-CoA kinase, GTP-dependent DPCK, kinase, dephosphocoenzyme A (phosphorylating), More, TK1697
ECTree
2.7.1.24 dephospho-CoA kinaseAdvanced search results
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Engineering on EC 2.7.1.24 - dephospho-CoA kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
R140K
the mutation results in a dramatic loss of catalytic activity
additional information
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
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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
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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
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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
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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
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additional information
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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
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