Information on EC 2.7.1.24 - dephospho-CoA kinase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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 ACCESSION NO.
LITERATURE
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram
active site, mechanism
-
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram
active site, mechanism
P44920
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
coenzyme A biosynthesis
-
Metabolic pathways
-
Pantothenate and CoA biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
ATP:3'-dephospho-CoA 3'-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
P63826
-
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
SEQUENCE CODE
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 ACCESSION NO.
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
P63826
-
-
-
?
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cysteine
-
activation; in vitro
cysteine
-
requirement
cysteine
-
activation; requirement
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0217
-
3'-Dephospho-CoA
P63826
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
P63826
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
P63826
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
P63826
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
P63826
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
P63826
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
P63826
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
P63826
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0345
-
ATP
P63826
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0501
-
ATP
P63826
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0568
-
ATP
P63826
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0575
-
ATP
P63826
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0598
-
ATP
P63826
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0639
-
ATP
P63826
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0867
-
ATP
P63826
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
0.003
-
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0017
-
3'-Dephospho-CoA
P63826
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
P63826
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
P63826
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
P63826
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
P63826
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
P63826
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
P63826
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
P63826
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.014
-
ATP
P63826
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0192
-
ATP
P63826
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.039
-
ATP
P63826
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.043
-
ATP
P63826
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0481
-
ATP
P63826
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.0651
-
ATP
P63826
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
0.067
-
ATP
P63826
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]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00034
-
3'-Dephospho-CoA
P63826
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.0015
-
3'-Dephospho-CoA
P63826
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.042
-
3'-Dephospho-CoA
P63826
mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.337
-
3'-Dephospho-CoA
P63826
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.38
-
3'-Dephospho-CoA
P63826
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.69
-
3'-Dephospho-CoA
P63826
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.703
-
3'-Dephospho-CoA
P63826
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.838
-
3'-Dephospho-CoA
P63826
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
3153
0.243
-
ATP
P63826
mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
22040
0.3
-
ATP
P63826
mutant enzyme L114A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
22040
0.448
-
ATP
P63826
mutant enzyme K14A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
22040
0.713
-
ATP
P63826
mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
22040
0.847
-
ATP
P63826
wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
22040
1.3
-
ATP
P63826
mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
22040
1.93
-
ATP
P63826
mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25C
22040
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-, Q13057
assay at
8
-
Q8MIR4
assay at
8.2
-
-
assay at
8.5
-
-
broad
8.5
-
-
recombinant enzyme, broad
8.5
-
P0A6I9
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-, Q13057
assay at
25
-
Q8MIR4
assay at
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
41
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.75
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
normal and Plasmodium lophurae-infected
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
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)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22000
-
-
monomeric enzyme form, gel filtration
22200
-
-
recombinant enzyme, gel filtration
25000
-
-
native enzyme, gel filtration
62000
-
-, Q13057
recombinant enzyme, gel filtration
62000
-
Q8MIR4
wild-type enzyme, gel filtration
66000
-
-
trimeric enzyme form, gel filtration
115000
-
-
gel filtration
118000
-
-
gel filtration
141000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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 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, 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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
2 min at 46C, inactivation
6.7
-
-
t1/2 at 46C: 2 min
10
-
-
2 min at 46C, 10% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
2 min, partially inactivated
46
-
-
t1/2: 2 min at pH 6.7, pH 10: 10% loss of activity, pH 5.5: 2 min, inactivation
50
-
-
2 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable to repeated freeze-thawing cycles
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
P63826
expressed in Escherichia coli B834(DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D32A
P63826
the mutant shows a catalytic efficiency of only 5% of the native enzyme
D32E
P63826
the mutant shows increased catalytic efficiency compared to the wild type enzyme
D32N
P63826
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
P63826
this mutation does not change either the Km or the Kcat of the reaction considerably
K14A
P63826
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
P63826
the mutation results in a decrease in the affinity of the enzyme for the acceptor substrate
R140A
P63826
this mutation completely abolishes kinetic activity
R140K
P63826
the mutation results in a dramatic loss of catalytic activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
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