Information on EC 2.7.1.24 - dephospho-CoA kinase:
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EC NUMBERCOMMENTARY
2.7.1.24-

RECOMMENDED NAMEGeneOntology No.
dephospho-CoA kinaseGO:0004140

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram		----
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram		active site, mechanismEscherichia coli-645079
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram		active site, mechanismHaemophilus influenzaeP44920645080

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
phospho group transfer----

PATHWAYKEGG LinkMetaCyc Link
coenzyme A biosynthesis-COA-PWY

SYSTEMATIC NAMEIUBMB Comments
ATP:3'-dephospho-CoA 3'-phosphotransferase-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3'-dephospho-CoA kinase----
dephosphocoenzyme A kinase----
dephosphocoenzyme A kinase (phosphorylating)----
DPCKHomo sapiens--643189, 671313, 672562
DPCKEscherichia coli--645079, 671313
DPCKAquifex aeolicus--671313
kinase, dephosphocoenzyme A (phosphorylating)----
additional informationSus scrofa-bifunctional enzyme is termed CoA-synthetase; bifunctional enzyme with phosphopantetheine adenylyltransferase activity, EC 2.7.7.3, and dephospho-CoA kinase activity, EC 2.7.1.24643177, 643178
additional informationHomo sapiensQ13057bifunctional enzyme is termed CoA synthase; bifunctional enzyme with phosphopantetheine adenylyltransferase activity, EC 2.7.7.3, and dephospho-CoA kinase activity, EC 2.7.1.24643189
additional informationSus scrofaQ8MIR4bifunctional enzyme with phosphopantetheine adenylyltransferase activity, EC 2.7.7.3, and dephospho-CoA kinase activity, EC 2.7.1.24643189

CAS REGISTRY NUMBERCOMMENTARY
9026-83-9-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Anas platyrhynchosduck4410, 645067--Manually annotated by BRENDA team
Aquifex aeolicus-671313--Manually annotated by BRENDA team
Columba sp.-643174, 645067, 645076--Manually annotated by BRENDA team
Corynebacterium ammoniagenes-643183--Manually annotated by BRENDA team
Corynebacterium ammoniagenesgene coaE645077--Manually annotated by BRENDA team
Escherichia coli-645079, 671313--Manually annotated by BRENDA team
Escherichia coligene caoE, formerly yacE645077P0A6I9SwissProtManually annotated by BRENDA team
Haemophilus influenzae-645080P44920UniprotManually annotated by BRENDA team
Homo sapiens-671313, 672562--Manually annotated by BRENDA team
Homo sapiensgene ppat/dpck, bifunctional enzyme with phosphopantetheine adenylyltransferase and dephospho-CoA kinase activities, termed CoA synthase643189Q13057SwissProtManually annotated by BRENDA team
Micrococcus luteus-4412--Manually annotated by BRENDA team
no activity in Plasmodium lophurae-4410--Manually annotated by BRENDA team
Rattus norvegicus-643174, 643176, 645076--Manually annotated by BRENDA team
Rattus norvegicusmale Wistar643179, 643180--Manually annotated by BRENDA team
Sus scrofa-643174, 643177, 643178, 645076--Manually annotated by BRENDA team
Sus scrofabifunctional enzyme with phosphopantetheine adenylyltransferase and dephospho-CoA kinase activities643189Q8MIR4SwissProtManually annotated by BRENDA team
Thermus thermophilusstrain HB8663357--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Haemophilus influenzaeP44920-645080---
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Thermus thermophilus--663357--?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Escherichia coli--645079-645079?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Escherichia coli--671313--?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Homo sapiens--672562--?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus--643174-643174-
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus--643179-643179-
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus--645076-645076?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus--643180-643180ir
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Sus scrofa--643174-643174?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Sus scrofa--643177-643177?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Sus scrofa--643178-643178?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Sus scrofa--645076-645076?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Micrococcus luteus--4412-4412?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Anas platyrhynchos--4410-4410?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Corynebacterium ammoniagenes--643183-643183?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Corynebacterium ammoniagenes--645077-645077ir
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Columba sp.--643174-643174?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Columba sp.--645076-645076?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Aquifex aeolicus--671313--?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Escherichia coliP0A6I9-645077-645077ir
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Homo sapiensQ13057-643189-643189?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Sus scrofaQ8MIR4-643189-643189?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus-specific643176-643176-
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Anas platyrhynchos, Columba sp.-specific645067-645067?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Anas platyrhynchos, Columba sp.-ITP or ADP are no substrates645067-645067?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus-no substrates are 3'-dephospho-alpha-carboxy-CoA643176-643176-
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Haemophilus influenzaeP44920last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety645080---
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Corynebacterium ammoniagenes-last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety645077-645077?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Escherichia coli-final step of coenzyme A biosynthesis645079--?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus-involved in coenzyme A biosynthesis, last irreversible reaction643180-643180?
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Thermus thermophilus-final step of coenzyme A biosynhesis663357--?
ATP + dephospho-tryptamine-CoAADP + tryptamine-CoA
show the reaction diagram		Homo sapiens--672562--?
additional information?-Anas platyrhynchos, Columba sp.-assay method: arsenolysis of dephospho-CoA, formation of CoA645067---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus, Sus scrofa--645076-645076
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Micrococcus luteus--4412-4412
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Corynebacterium ammoniagenes--643183-643183
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Columba sp.--645076-645076
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Haemophilus influenzaeP44920last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety645080--
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Corynebacterium ammoniagenes-last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety645077-645077
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Escherichia coli-final step of coenzyme A biosynthesis645079--
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Rattus norvegicus-involved in coenzyme A biosynthesis, last irreversible reaction643180-643180
ATP + dephospho-CoAADP + CoA
show the reaction diagram		Thermus thermophilus-final step of coenzyme A biosynhesis663357--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
ATPAnas platyrhynchos, Columba sp.-requirement645067 2D-image
ATPAquifex aeolicus, Escherichia coli--671313 2D-image
ATPHomo sapiens--672562 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
H2SColumba sp., Rattus norvegicus, Sus scrofa-activation, in vitro643174
Mg2+Micrococcus luteus-requirement4412
Mg2+Columba sp., Rattus norvegicus, Sus scrofa-2 mM; requirement643174
Mg2+Rattus norvegicus-0.5 mM; requirement643176
Mg2+Rattus norvegicus-requirement643179, 645076
Mg2+Rattus norvegicus-Km-value: 0.5 mM; requirement643180
Mg2+Columba sp.-requirement645067, 645076
Mg2+Anas platyrhynchos-requirement645067
Mg2+Sus scrofa-requirement645076

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
coenzyme ARattus norvegicus--643180 2D-image
deoxycholateRattus norvegicus-inactivation, 0.2%643176 2D-image
additional informationColumba sp.-no inhibition by F- with or without phosphate, adenosine, 2-, 3- or 5-adenylic acids, ADP, NAD+, NADH, deamino-NAD+, adenosine diphosphate ribose645067-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
cysteineColumba sp., Rattus norvegicus, Sus scrofa-activation; in vitro643174 2D-image
cysteineRattus norvegicus-requirement643176 2D-image
cysteineAnas platyrhynchos, Columba sp.-activation; requirement645067 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.05-ATPRattus norvegicus--643179 2D-image
0.1-ATPRattus norvegicus-cytosolic enzyme643179 2D-image
0.14-ATPCorynebacterium ammoniagenes-native wild-type enzyme, pH 8.5, 25°C645077 2D-image
0.19-ATPHomo sapiensQ13057recombinant enzyme, pH 8.0, 25°C643189 2D-image
0.33-ATPSus scrofaQ8MIR4recombinant enzyme, pH 8.0, 25°C643189 2D-image
0.36-ATPRattus norvegicus--643176 2D-image
0.003-dephospho-CoAColumba sp.-pH 8.2, 37°C645067 2D-image
0.0041-dephospho-CoASus scrofaQ8MIR4native enzyme, pH 8.0, 25°C643189 2D-image
0.0052-dephospho-CoAHomo sapiensQ13057recombinant enzyme, pH 8.0, 25°C643189 2D-image
0.01-dephospho-CoARattus norvegicus-mitochondrial enzyme643179 2D-image
0.01-dephospho-CoARattus norvegicus--643180 2D-image
0.12-dephospho-CoARattus norvegicus--643176 2D-image
0.76-dephospho-CoACorynebacterium ammoniagenes-native wild-type enzyme, pH 8.5, 25°C645077 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.038-Corynebacterium ammoniagenes--643183
0.346-Rattus norvegicus--643176
3.68-Sus scrofa--643177
6.5-Corynebacterium ammoniagenes-purified native wild-type enzyme645077
22-Corynebacterium ammoniagenes-purified recombinant wild-type enzyme645077
additional information-Anas platyrhynchos-specific activity per mg hemoglobin4410
additional information-Micrococcus luteus--4412
additional information-Columba sp.--645067
additional information-Aquifex aeolicus-145.5 units/mg671313

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
8-Homo sapiensQ13057assay at643189
8-Sus scrofaQ8MIR4assay at643189
8.2-Columba sp.-assay at645067
8.5-Rattus norvegicus-broad643179
8.5-Corynebacterium ammoniagenes-recombinant enzyme, broad645077
8.5-Escherichia coliP0A6I9-645077
9-Columba sp., Rattus norvegicus, Sus scrofa--643174
9-Rattus norvegicus--643180
10-Rattus norvegicus--643176

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Homo sapiensQ13057assay at643189
25-Sus scrofaQ8MIR4assay at643189
25-Corynebacterium ammoniagenes-assay at645077
30-Sus scrofa-assay at643177
30-Rattus norvegicus-assay at643179
37-Columba sp., Rattus norvegicus, Sus scrofa-assay at643174
37-Rattus norvegicus-assay at643176
37-Anas platyrhynchos, Columba sp.-assay at645067
41-Anas platyrhynchos-assay at4410

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.75-Sus scrofa--643177

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
erythrocyteAnas platyrhynchos-normal and Plasmodium lophurae-infected4410Manually annotated by BRENDA team
Hep-G2 cellHomo sapiensQ13057-643189Manually annotated by BRENDA team
liverRattus norvegicus--643174, 643176, 643179, 643180Manually annotated by BRENDA team
liverSus scrofa--643174, 643177, 643178, 643189Manually annotated by BRENDA team
liverColumba sp.--643174, 645067Manually annotated by BRENDA team
liverAnas platyrhynchos--645067Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytosolAnas platyrhynchos--58294410Manually annotated by BRENDA team
cytosolMicrococcus luteus--58294412Manually annotated by BRENDA team
cytosolRattus norvegicus--5829643174, 643176, 643179, 643180Manually annotated by BRENDA team
cytosolSus scrofa--5829643174, 643177, 643189Manually annotated by BRENDA team
cytosolColumba sp.--5829643174Manually annotated by BRENDA team
cytosolCorynebacterium ammoniagenes--5829643183Manually annotated by BRENDA team
mitochondrionColumba sp.--5739643174, 645067Manually annotated by BRENDA team
mitochondrionRattus norvegicus, Sus scrofa--5739643174Manually annotated by BRENDA team
mitochondrionRattus norvegicus-inner membrane5739643179Manually annotated by BRENDA team
mitochondrionRattus norvegicus-intramitochondrial localization5739643180Manually annotated by BRENDA team
mitochondrionAnas platyrhynchos--5739645067Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2if2, downloadSCOP (2if2)CATH (2if2)Aquifex aeolicus (strain VF5)
1n3b, downloadSCOP (1n3b)CATH (1n3b)Escherichia coli (strain K12)
1t3h, downloadSCOP (1t3h)CATH (1t3h)Escherichia coli (strain K12)
1vhl, downloadSCOP (1vhl)CATH (1vhl)Escherichia coli (strain K12)
1vht, downloadSCOP (1vht)CATH (1vht)Escherichia coli (strain K12)
1viy, downloadSCOP (1viy)CATH (1viy)Escherichia coli (strain K12)
1jjv, downloadSCOP (1jjv)CATH (1jjv)Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
2grj, downloadSCOP (2grj)CATH (2grj)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
22000-Escherichia coli-monomeric enzyme form, gel filtration645079
22200-Corynebacterium ammoniagenes-recombinant enzyme, gel filtration645077
25000-Corynebacterium ammoniagenes-native enzyme, gel filtration645077
62000-Homo sapiensQ13057recombinant enzyme, gel filtration643189
62000-Sus scrofaQ8MIR4wild-type enzyme, gel filtration643189
66000-Escherichia coli-trimeric enzyme form, gel filtration645079
115000-Sus scrofa-gel filtration643177
118000-Sus scrofa-gel filtration643178

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Escherichia coliP0A6I91 * 22600, deduced from DNA sequence645077
dimerSus scrofa-2 * 57000, SDS-PAGE643177
dimerSus scrofa-2 * 61000, SDS-PAGE, subunit structure643178
monomerSus scrofaQ8MIR41 * 60000, SDS-PAGE643189
trimerThermus thermophilus-3 * 22700, three monomers in an asymmetric unit, crystal structure analysis, monomer weight calculated from the deduced amino acid sequence663357
monomerCorynebacterium ammoniagenes-1 * 22200, recombinant wild-type enzyme, SDS-PAGE; 1 * 25000, native wild-type enzyme, SDS-PAGE645077
additional informationEscherichia coli-enzyme is a monomer in solution, but crystallizes as a tightly packed trimer, in presence of stabilizing sulfate ions the monomeric and trimeric forms build an equilibrium in solution645079

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
hanging drop vapour diffusion method, purified enzyme in 20 mM Tris-HCl, pH 7.5, 0.2 M NaCl, 5% glycerol v/v, 10 mM DTT, from droplets of equal volume of protein solution and reservoir solution, reservoir solution: 20% w/v PEG 8K, 50 mM cacodylate, pH 6.5, 0.2 M (NH4)2SO4, 5% glycerol v/v, 21°C, within 4 days to 2 weeks, X-ray and light scattering structure determination and analysisEscherichia coli-645079
in complex with ATP, structure determination and analysisHaemophilus influenzaeP44920645080
hanging drop vapor diffusion methodThermus thermophilus-663357

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
5.5-Rattus norvegicus-2 min at 46°C, inactivation643176
6.7-Rattus norvegicus-t1/2 at 46°C: 2 min643176
10-Rattus norvegicus-2 min at 46°C, 10% loss of activity643176

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
40-Rattus norvegicus-2 min, partially inactivated643176
46-Rattus norvegicus-t1/2: 2 min at pH 6.7, pH 10: 10% loss of activity, pH 5.5: 2 min, inactivation643176
50-Rattus norvegicus-2 min, inactivation643176

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
stable to repeated freeze-thawing cyclesColumba sp.-645067

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-15°C, partially purified preparation, at least 2 monthsColumba sp.-645067
-20°C, 0.5 mg protein/ml, at least 1 monthSus scrofa-643177
frozen, partially purified preparation, quite stableSus scrofa-643174

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4.5fold from liver acetone powderColumba sp.-645067
native wild-type enzyme, 2800fold to homogeneity; recombinant wild-type from Escherichia coli W3110, 22foldCorynebacterium ammoniagenes-645077
partial, distinct from EC 2.7.7.3Corynebacterium ammoniagenes-643183
recombinant His-tagged enzyme from strain DL41Escherichia coli-645079
recombinant from Escherichia coliHomo sapiensQ13057643189
-Rattus norvegicus-643176
-Sus scrofa-643177, 643189
partialSus scrofa-643174
recombinant enzymeThermus thermophilus-663357

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expressed in Escherichia coli strain BL21(DE3)Aquifex aeolicus-671313
gene coaE, DNA sequence determination and analysis, overexpression in Escherichia coli strain W3110Corynebacterium ammoniagenes-645077
expressed in Escherichia coli strain BL21(DE3)Escherichia coli-671313
gene coaE, expression as His-tagged protein in strain DL41Escherichia coli-645079
gene yacE, DNA sequence analysisEscherichia coliP0A6I9645077
-Haemophilus influenzaeP44920645080
gene ppat/dpck encoding bifunctional enzyme with phosphopantetheine adenylyltransferase and dephospho-CoA kinase activity, located on chromosome 17q12-21, DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3)Homo sapiensQ13057643189
expressed in Escherichia coli B834(DE3)Thermus thermophilus-663357

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
analysisAquifex aeolicus, Escherichia coli, Homo sapiens-dephospho-CoA kinase provides a rapid and sensitive radiochemical assay for coenzyme A and its thioesters. The DPCK method can be applied accurately to pools of CoA metabolites isolated from cellular material671313

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
TuberculosisInsights into the regulatory characteristics of the mycobacterial dephosphocoenzyme A kinase: implications for the universal CoA biosynthesis pathway. PubMed
TuberculosisThe role of UPF0157 in the folding of M. tuberculosis dephosphocoenzyme A kinase and the regulation of the latter by CTP. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
4410Brohn, F.H.; Trager, W.Coenzyme A requirement of malaria parasites: enzymes of coenzyme A biosynthesis in normal duck erythrocytes and erythrocytes infected with Plasmodium lophuraeProc. Natl. Acad. Sci. USA722456-24581975Anas platyrhynchos, no activity in Plasmodium lophurae PubMed
4412Nishimura, N.; Kakimoto, T.; Chibata, I.Mechanism of coenzyme A biosynthesis by Sarcina luteaJ. Ferment. Technol.6195-991983Micrococcus luteus-
643174Hoagland, M.B.; Novelli, G.D.Biosynthesis of coenzyme A from phosphopantetheine from pantothenateJ. Biol. Chem.207767-7731954Columba sp., Rattus norvegicus, Sus scrofa PubMed
643176Abiko, 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.18A358-3641970Rattus norvegicus-
643177Worrall, D.M.; Tubbs, P.K.A bifunctional enzyme complex in coenzyme A biosynthesis: purification of pantetheine phosphate adenylyltransferase and dephospho-CoA kinaseBiochem. J.215153-1571983Sus scrofa PubMed
643178Worrall, D.M.; Lambert, S.F.; Tubbs, P.K.Limited proteolysis of pig liver CoA synthase: evidence for subunit identityFEBS Lett.187277-2791985Sus scrofa PubMed
643179Skrede, S.; Halvorsen, O.Mitochondrial biosynthesis of coenzyme ABiochem. Biophys. Res. Commun.911536-15421979Rattus norvegicus PubMed
643180Skrede, S.; Halvorsen, O.Mitochondrial pantetheinephosphate adenylyltransferase and dephospho-CoA kinaseEur. J. Biochem.13157-631983Rattus norvegicus PubMed
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.24)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)