Information on EC 2.7.1.24 - dephospho-CoA kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.7.1.24
-
RECOMMENDED NAME
GeneOntology No.
dephospho-CoA kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram
active site, mechanism
P44920
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram
active site, mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme A biosynthesis I
-
-
coenzyme A biosynthesis II (mammalian)
-
-
coenzyme A metabolism
-
-
Metabolic pathways
-
-
Pantothenate and CoA biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:3'-dephospho-CoA 3'-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3'-dephospho-CoA kinase
-
-
-
-
coenzyme A synthase
-
a bifunctional enzyme that also shows dephosphocoenzyme A kinase activity
dephosphocoenzyme A kinase
-
-
-
-
dephosphocoenzyme A kinase
-
-
dephosphocoenzyme A kinase
-
-
dephosphocoenzyme A kinase
P9WPA3
-
dephosphocoenzyme A kinase (phosphorylating)
-
-
-
-
DPCK
Q13057
-
kinase, dephosphocoenzyme A (phosphorylating)
-
-
-
-
additional information
Q13057
bifunctional enzyme is termed CoA synthase; bifunctional enzyme with phosphopantetheine adenylyltransferase activity, EC 2.7.7.3, and dephospho-CoA kinase activity, EC 2.7.1.24
additional information
-
bifunctional enzyme is termed CoA-synthetase; bifunctional enzyme with phosphopantetheine adenylyltransferase activity, EC 2.7.7.3, and dephospho-CoA kinase activity, EC 2.7.1.24
additional information
Q8MIR4
bifunctional enzyme with phosphopantetheine adenylyltransferase activity, EC 2.7.7.3, and dephospho-CoA kinase activity, EC 2.7.1.24
CAS REGISTRY NUMBER
COMMENTARY
9026-83-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene caoE, formerly yacE
SwissProt
Manually annotated by BRENDA team
gene ppat/dpck, bifunctional enzyme with phosphopantetheine adenylyltransferase and dephospho-CoA kinase activities, termed CoA synthase
SwissProt
Manually annotated by BRENDA team
no activity in Plasmodium lophurae
-
-
-
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
bifunctional enzyme with phosphopantetheine adenylyltransferase and dephospho-CoA kinase activities
SwissProt
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3'-dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
?
ATP + 3'-dephospho-CoA
ADP + CoA
show the reaction diagram
P9WPA3
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
P44920
-
-
-
-
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
ir
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
ir
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
P0A6I9
-
-
ir
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
Q13057
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
Q8MIR4
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
specific
-
-
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
specific
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
ITP or ADP are no substrates
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
no substrates are 3'-dephospho-alpha-carboxy-CoA
-
-
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
P44920
last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety
-
-
-
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
final step of coenzyme A biosynthesis
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
involved in coenzyme A biosynthesis, last irreversible reaction
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
final step of coenzyme A biosynhesis
-
-
?
ATP + dephospho-tryptamine-CoA
ADP + tryptamine-CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
assay method: arsenolysis of dephospho-CoA, formation of CoA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
P44920
last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety
-
-
-
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
last step of coenzyme A biosynthesis: phosphorylation of the 3'-OH group of the ribose sugar moiety
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
final step of coenzyme A biosynthesis
-
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
involved in coenzyme A biosynthesis, last irreversible reaction
-
?
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
-
final step of coenzyme A biosynhesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H2S
-
activation, in vitro
Mg2+
-
requirement
Mg2+
-
2 mM; requirement
Mg2+
-
0.5 mM; requirement
Mg2+
-
Km-value: 0.5 mM; requirement
Mg2+
-
requirement
Mg2+
-
requirement
Mg2+
-
requirement
Mg2+
-
requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
coenzyme A
-
-
CTP
-
enzymatic activity is regulated by CTP which strongly binds the enzyme at a site overlapping that of the leading substrate, dephosphocoenzyme A, thereby obscuring the binding site and limiting catalysis. 16% residual activity at 1 mM CTP
deoxycholate
-
inactivation, 0.2%
EDC4
-
EDC4 is also known as Ge-1, Hedls, RCD-8. EDC4 strongly inhibits the dephospho-CoA kinase activity of coenzyme A synthase in vitro
-
additional information
-
no inhibition by F- with or without phosphate, adenosine, 2-, 3- or 5-adenylic acids, ADP, NAD+, NADH, deamino-NAD+, adenosine diphosphate ribose
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
activation; in vitro
cysteine
-
requirement
cysteine
-
activation; requirement
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0217
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0349
3'-Dephospho-CoA
P9WPA3
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0372
3'-Dephospho-CoA
P9WPA3
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0758
3'-Dephospho-CoA
P9WPA3
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0809
3'-Dephospho-CoA
P9WPA3
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0877
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.181
3'-Dephospho-CoA
P9WPA3
mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.501
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0345
ATP
P9WPA3
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.05
ATP
-
-
0.0501
ATP
P9WPA3
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0568
ATP
P9WPA3
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0575
ATP
P9WPA3
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0598
ATP
P9WPA3
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0639
ATP
P9WPA3
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0867
ATP
P9WPA3
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.1
ATP
-
cytosolic enzyme
0.14
ATP
-
native wild-type enzyme, pH 8.5, 25C
0.19
ATP
Q13057
recombinant enzyme, pH 8.0, 25C
0.33
ATP
Q8MIR4
recombinant enzyme, pH 8.0, 25C
0.36
ATP
-
-
0.003
dephospho-CoA
-
pH 8.2, 37C
0.0041
dephospho-CoA
Q8MIR4
native enzyme, pH 8.0, 25C
0.0052
dephospho-CoA
Q13057
recombinant enzyme, pH 8.0, 25C
0.01
dephospho-CoA
-
mitochondrial enzyme
0.01
dephospho-CoA
-
-
0.12
dephospho-CoA
-
-
0.76
dephospho-CoA
-
native wild-type enzyme, pH 8.5, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0076
3'-Dephospho-CoA
P9WPA3
mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0255
3'-Dephospho-CoA
P9WPA3
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0257
3'-Dephospho-CoA
P9WPA3
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0293
3'-Dephospho-CoA
P9WPA3
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0327
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0334
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0569
3'-Dephospho-CoA
P9WPA3
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.014
ATP
P9WPA3
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0192
ATP
P9WPA3
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.039
ATP
P9WPA3
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.043
ATP
P9WPA3
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0481
ATP
P9WPA3
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0651
ATP
P9WPA3
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.067
ATP
P9WPA3
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00034
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.0015
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.042
3'-Dephospho-CoA
P9WPA3
mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.337
3'-Dephospho-CoA
P9WPA3
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.38
3'-Dephospho-CoA
P9WPA3
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.69
3'-Dephospho-CoA
P9WPA3
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.703
3'-Dephospho-CoA
P9WPA3
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.838
3'-Dephospho-CoA
P9WPA3
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
1814
0.243
ATP
P9WPA3
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
4
0.3
ATP
P9WPA3
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
4
0.448
ATP
P9WPA3
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
4
0.713
ATP
P9WPA3
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
4
0.847
ATP
P9WPA3
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
4
1.3
ATP
P9WPA3
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
4
1.93
ATP
P9WPA3
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.68
-
-
6.5
-
purified native wild-type enzyme
22
-
purified recombinant wild-type enzyme
additional information
-
specific activity per mg hemoglobin
additional information
-
-
additional information
-
-
additional information
-
145.5 units/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
Q13057
assay at
8
Q8MIR4
assay at
8.2
-
assay at
8.5
-
recombinant enzyme, broad
8.5
P0A6I9
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
Q13057
assay at
25
Q8MIR4
assay at
30
-
assay at
30
-
assay at
37
-
assay at
41
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.75
-
-
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
-
monomeric enzyme form, gel filtration
645079
22200
-
recombinant enzyme, gel filtration
645077
25000
-
native enzyme, gel filtration
645077
62000
Q13057
recombinant enzyme, gel filtration
643189
62000
Q8MIR4
wild-type enzyme, gel filtration
643189
66000
-
trimeric enzyme form, gel filtration
645079
115000
-
gel filtration
643177
118000
-
gel filtration
643178
141000
-
gel filtration
723532
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
P0A6I9
1 * 22600, deduced from DNA sequence
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE, subunit structure
homotrimer
-
3 * 47000, SDS-PAGE
monomer
Q8MIR4
1 * 60000, SDS-PAGE
trimer
-
3 * 22700, three monomers in an asymmetric unit, crystal structure analysis, monomer weight calculated from the deduced amino acid sequence
monomer
-
1 * 22200, recombinant wild-type enzyme, SDS-PAGE, 1 * 25000, native wild-type enzyme, SDS-PAGE
additional information
-
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 solution
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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, 21C, within 4 days to 2 weeks, X-ray and light scattering structure determination and analysis
-
in complex with ATP, structure determination and analysis
P44920
hanging drop vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
2 min at 46C, inactivation
643176
6.7
-
t1/2 at 46C: 2 min
643176
10
-
2 min at 46C, 10% loss of activity
643176
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
2 min, partially inactivated
643176
46
-
t1/2: 2 min at pH 6.7, pH 10: 10% loss of activity, pH 5.5: 2 min, inactivation
643176
50
-
2 min, inactivation
643176
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to repeated freeze-thawing cycles
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, partially purified preparation, at least 2 months
-
-20C, 0.5 mg protein/ml, at least 1 month
-
frozen, partially purified preparation, quite stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4.5fold from liver acetone powder
-
native wild-type enzyme, 2800fold to homogeneity; recombinant wild-type from Escherichia coli W3110, 22fold
-
partial, distinct from EC 2.7.7.3
-
recombinant His-tagged enzyme from strain DL41
-
recombinant from Escherichia coli
Q13057
partial
-
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)
-
gene coaE, DNA sequence determination and analysis, overexpression in Escherichia coli strain W3110
-
expressed in Escherichia coli strain BL21(DE3)
-
gene coaE, expression as His-tagged protein in strain DL41
-
gene yacE, DNA sequence analysis
P0A6I9
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)
Q13057
expressed in Escherichia coli BL21(DE3) cells
P9WPA3
expressed in Escherichia coli B834(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D32A
P9WPA3
the mutant shows a catalytic efficiency of only 5% of the native enzyme
D32E
P9WPA3
the mutant shows increased catalytic efficiency compared to the wild type enzyme
D32N
P9WPA3
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
P9WPA3
this mutation does not change either the Km or the Kcat of the reaction considerably
K14A
P9WPA3
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
P9WPA3
the mutation results in a decrease in the affinity of the enzyme for the acceptor substrate
R140A
P9WPA3
this mutation completely abolishes kinetic activity
R140K
P9WPA3
the mutation results in a dramatic loss of catalytic activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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 material