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 hide
2.7.1.24
-
RECOMMENDED NAME
GeneOntology No.
dephospho-CoA kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 3'-dephospho-CoA = ADP + CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme A biosynthesis I
-
-
coenzyme A biosynthesis II (mammalian)
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-
coenzyme A metabolism
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-
Metabolic pathways
-
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Pantothenate and CoA biosynthesis
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-
SYSTEMATIC NAME
IUBMB Comments
ATP:3'-dephospho-CoA 3'-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-83-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
duck
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Plasmodium lophurae
-
-
-
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3'-dephospho-CoA
ADP + CoA
show the reaction diagram
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
ATP + dephospho-tryptamine-CoA
ADP + tryptamine-CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + dephospho-CoA
ADP + CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A
-
-
CTP
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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
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inactivation, 0.2%
EDC4
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EDC4 is also known as Ge-1, Hedls, RCD-8. EDC4 strongly inhibits the dephospho-CoA kinase activity of coenzyme A synthase in vitro
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0217 - 0.501
3'-Dephospho-CoA
0.0345 - 0.36
ATP
0.003 - 0.76
dephospho-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.0569
3'-Dephospho-CoA
0.014 - 0.067
ATP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00034 - 0.838
3'-Dephospho-CoA
0.243 - 1.93
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.68
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-
6.5
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purified native wild-type enzyme
22
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purified recombinant wild-type enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.75
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-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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normal and Plasmodium lophurae-infected
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / 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 hide
LITERATURE
22000
-
monomeric enzyme form, gel filtration
22200
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recombinant enzyme, gel filtration
25000
-
native enzyme, gel filtration
66000
-
trimeric enzyme form, gel filtration
115000
-
gel filtration
118000
-
gel filtration
141000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
1 * 22600, deduced from DNA sequence
homotrimer
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3 * 47000, SDS-PAGE
monomer
trimer
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3 * 22700, three monomers in an asymmetric unit, crystal structure analysis, monomer weight calculated from the deduced amino acid sequence
additional information
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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
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in complex with ATP, structure determination and analysis
hanging drop vapor diffusion method
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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2 min at 46C, inactivation
643176
6.7
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t1/2 at 46C: 2 min
643176
10
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2 min at 46C, 10% loss of activity
643176
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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2 min, partially inactivated
46
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t1/2: 2 min at pH 6.7, pH 10: 10% loss of activity, pH 5.5: 2 min, inactivation
50
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2 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to repeated freeze-thawing cycles
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, partially purified preparation, at least 2 months
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-20C, 0.5 mg protein/ml, at least 1 month
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frozen, partially purified preparation, quite stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4.5fold from liver acetone powder
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native wild-type enzyme, 2800fold to homogeneity; recombinant wild-type from Escherichia coli W3110, 22fold
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partial
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partial, distinct from EC 2.7.7.3
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recombinant enzyme
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recombinant from Escherichia coli
recombinant His-tagged enzyme from strain DL41
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834(DE3)
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain BL21(DE3)
gene coaE, DNA sequence determination and analysis, overexpression in Escherichia coli strain W3110
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gene coaE, expression as His-tagged protein in strain DL41
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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)
gene yacE, DNA sequence analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
R140A
this mutation completely abolishes kinetic activity
R140K
the mutation results in a dramatic loss of catalytic activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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