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The enzyme appears in viruses and cellular organisms
Synonyms adenylate kinase 4, gtp:amp phosphotransferase, adenylate kinase 3, csak3, more
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GTP: AMP phosphotra nsferase
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GTP:AMP phosphotransferase
guanosine triphosphate-adenylate kinase
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kinase, nucleoside triphosphate-adenylate (phosphorylating)
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nucleoside triphosphate-adenosine monophosphate transphosphorylase
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nucleoside triphosphate-adenylate kinase
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ssozyme 3 of adenylate kinase
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AK3
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GTP:AMP phosphotransferase
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GTP:AMP phosphotransferase
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nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
mechanism
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nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
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phospho group transfer
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nucleoside-triphosphate:AMP phosphotransferase
Many nucleoside triphosphates can act as donors.
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AMP + GTP
ADP + GDP
Substrates: - Products: -
?
dGTP + dAMP
dGDP + dADP
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Substrates: - Products: -
r
GTP + IMP
GDP + IDP
Q964H2
Substrates: - Products: -
?
nucleoside triphosphate + AMP
nucleoside diphosphate + ADP
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Substrates: involved in reaction sequence of substrate level phosphorylation Products: -
r
additional information
?
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ATP + AMP
2 ADP
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Substrates: - Products: -
r
ATP + AMP
2 ADP
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Substrates: poor substrate, highly specific for AMP, phosphorylation at about 5% the rate of ITP Products: -
r
ATP + AMP
2 ADP
Q964H2
Substrates: - Products: -
?
CTP + AMP
CDP + ADP
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Substrates: - Products: -
r
CTP + AMP
CDP + ADP
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Substrates: highly specific for AMP, phosphorylation at about 11% the rate of ITP Products: -
r
CTP + AMP
CDP + ADP
Q964H2
Substrates: - Products: -
?
GTP + AMP
GDP + ADP
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Substrates: - Products: -
?
GTP + AMP
GDP + ADP
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Substrates: - Products: -
r
GTP + AMP
GDP + ADP
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Substrates: highly specific for AMP and ADP, in reverse reaction Products: via nucleotide-enzyme complex, no phosphorylated enzyme intermediate
r
GTP + AMP
GDP + ADP
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Substrates: not: CMP, GMP, IMP, UMP Products: -
r
GTP + AMP
GDP + ADP
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Substrates: phosphorylation at about 90% the rate of ITP Products: via nucleotide-enzyme complex, no phosphorylated enzyme intermediate
r
GTP + AMP
GDP + ADP
Substrates: - Products: -
?
GTP + AMP
GDP + ADP
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Substrates: - Products: -
r
GTP + AMP
GDP + ADP
Q964H2
Substrates: - Products: -
?
GTP + AMP
GDP + ADP
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Substrates: - Products: -
?
GTP + AMP
GDP + ADP
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Substrates: no acceptor substrates are 2'-AMP, 3'-AMP Products: -
r
GTP + AMP
GDP + ADP
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Substrates: not: CMP, GMP, IMP, UMP Products: -
r
GTP + AMP
GDP + ADP
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Substrates: dAMP can replace AMP Products: -
r
ITP + AMP
IDP + ADP
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Substrates: best substrate Products: via nucleotide-enzyme complex, no phosphorylated enzyme intermediate
r
ITP + AMP
IDP + ADP
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Substrates: highly specific for AMP and ADP in reverse reaction Products: via nucleotide-enzyme complex, no phosphorylated enzyme intermediate
r
ITP + AMP
IDP + ADP
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Substrates: no donor substrate is ribose 5'-triphosphate Products: -
r
ITP + AMP
IDP + ADP
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Substrates: not: GMP Products: -
r
ITP + AMP
IDP + ADP
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Substrates: no acceptor substrates are 3'-GMP Products: via nucleotide-enzyme complex, no phosphorylated enzyme intermediate
r
ITP + AMP
IDP + ADP
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Substrates: not: IMP, CMP, UMP Products: -
r
ITP + AMP
IDP + ADP
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Substrates: not: IMP, CMP, UMP Products: via nucleotide-enzyme complex, no phosphorylated enzyme intermediate
r
ITP + AMP
IDP + ADP
Q964H2
Substrates: - Products: -
?
ITP + AMP
IDP + ADP
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Substrates: dAMP can replace AMP Products: -
r
ITP + AMP
IDP + ADP
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Substrates: not: dCMP, dGMP, TDP, deoxyadenosine Products: -
r
UTP + AMP
UDP + ADP
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Substrates: - Products: -
r
UTP + AMP
UDP + ADP
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Substrates: highly specific for AMP, phosphorylation at about 19% the rate of ITP Products: -
r
UTP + AMP
UDP + ADP
Q964H2
Substrates: - Products: -
?
additional information
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Q964H2
Substrates: GTP + GMP/CMP/UMP activity below 1%, ATP + AMP activity below 1% Products: -
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additional information
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Substrates: GTP + GMP/CMP/UMP activity below 1%, ATP + AMP activity below 1% Products: -
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additional information
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Substrates: the enzyme does not accept ATP as a substrate Products: -
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additional information
?
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Substrates: ATP + AMP no significant formation of ADP Products: -
?
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GTP + AMP
GDP + ADP
Substrates: - Products: -
?
nucleoside triphosphate + AMP
nucleoside diphosphate + ADP
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Substrates: involved in reaction sequence of substrate level phosphorylation Products: -
r
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Ca2+
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activation, 50% as effective as Mg2+
Fe
Q964H2
0.3 mol Fe/mol protein
additional information
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no activation by EDTA, cysteamine, GSH or high phosphate concentrations
Mg2+
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requirement, 5-10 mM
Mg2+
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actual substrate: MgNTP
Mg2+
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activation, 4 mM, as good as Mn2+, slightly inhibitory above 4 mM
Mg2+
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actual substrate: MgNTP
Mn2+
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activation, as good as Mg2+
Mn2+
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75% as effective as Mg2+
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(Adenylyl)5-adenosine
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ADP
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reverse reaction, kinetics
AMP
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free form, Mg2+ reverses
GDP
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reverse reaction, kinetics
guanosine(5')pentaphospho(5')adenosine
Q964H2
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Mg2+
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weak, above 4 mM, activates below
p-hydroxymercuribenzoate
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weak
P1,P5-di(adenosine-5')pentaphosphate
P1,P5-di(adenosine-5')pentaphosphate
more than 70% inhibition by 2.0 mM
P1,P5-di(adenosine-5')pentaphosphate
Q964H2
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additional information
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no inhibition by EDTA, GSH, cysteamine or high phosphate concentrations
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additional information
Q964H2
not inhibitory at concentrations up to 1 mM: chloroquine, primaquine, artemisinine, mefloquine
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additional information
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not inhibitory at concentrations up to 1 mM: chloroquine, primaquine, artemisinine, mefloquine
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Adenocarcinoma of Lung
Adenylate kinase 4 modulates oxidative stress and stabilizes HIF-1? to drive lung adenocarcinoma metastasis.
Breast Neoplasms
Adenylate Kinase 4 Modulates the Resistance of Breast Cancer Cells to Tamoxifen through an m6A-Based Epitranscriptomic Mechanism.
Breast Neoplasms
ATF3 Modulates the Resistance of Breast Cancer Cells to Tamoxifen through an N6-Methyladenosine-Based Epitranscriptomic Mechanism.
Carcinogenesis
Adenylate kinase 4 promotes bladder cancer cell proliferation and invasion.
Clonorchiasis
Recombinant adenylate kinase 3 from liver fluke Clonorchis sinensis for histochemical analysis and serodiagnosis of clonorchiasis.
Lung Neoplasms
Adenylate kinase 4 modulates oxidative stress and stabilizes HIF-1? to drive lung adenocarcinoma metastasis.
Malaria
Subcellular localization of adenylate kinases in Plasmodium falciparum.
Neoplasm Metastasis
Adenylate kinase 4 modulates oxidative stress and stabilizes HIF-1? to drive lung adenocarcinoma metastasis.
Neoplasms
Adenylate kinase 4 promotes bladder cancer cell proliferation and invasion.
Neoplasms
Identification of specific protein markers in microdissected hepatocellular carcinoma.
Neoplasms
Modulation of anti-cancer drug sensitivity through the regulation of mitochondrial activity by adenylate kinase 4.
Ovarian Neoplasms
Identification of AK4 as a novel therapeutic target for serous ovarian cancer.
Urinary Bladder Neoplasms
Adenylate kinase 4 promotes bladder cancer cell proliferation and invasion.
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0.29
ADP
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pH 8.0, with GDP
1
ATP
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pH 8.0, with of AMP
9.1
CTP
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pH 8.0, with of AMP
0.0012
GDP
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pH 8.0, with ADP
0.63
ITP
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pH 8.0, with AMP
7.4
UTP
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pH 8.0, with of AMP
additional information
ATP
0.033
AMP
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0.056
GTP
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pH 8.0, with AMP
additional information
ATP
Q964H2
Km for ATP more than 5 mM
additional information
ATP
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Km for ATP more than 5 mM
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0.00014 - 0.00021
guanosine(5')pentaphospho(5')adenosine
0.0114
P1,P5-di(adenosine-5')pentaphosphate
Q964H2
25°C, pH 6
0.73
ATP
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pH 8.5, competitive with AMP
0.74
ATP
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pH 8.5, competitive with GTP
0.00014
guanosine(5')pentaphospho(5')adenosine
Q964H2
25°C, pH 6
0.00021
guanosine(5')pentaphospho(5')adenosine
Q964H2
25°C, pH 7.4
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0.1
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native isoenzyme Adk2p (long) 30°C
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7.5
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in presence of ITP + AMP
8.5
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7 - 9.7
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about half-maximal activity at pH 7 and 9.7
6 - 9
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half-maximal activity at pH 6 and pH 9
6 - 9
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about half-maximal activity at pH 6 and about 80% of maximal activity at pH 9
6 - 9
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at pH 4.5 the activity is about 2% of that at pH 7.4
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30
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soluble isoenzyme Adk2p (short)
35 - 55
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soluble isoenzyme Adk2p (long)
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SwissProt
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strains BY4741 and D273-10B
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calf
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UniProt
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SwissProt
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strains HB3 and Dd2
Q964H2
SwissProt
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highest in adult stage among three stages of life cycle (expression scores of CsAK3 in egg stage:metacercariae stage:adult stage = 0:2:6)
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the enzyme is localized to the subtegumental tissue of Clonorchis sinensis and is excreted into the bile duct of the host
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highest in adult stage among three stages of life cycle (expression scores of CsAK3 in egg stage:metacercariae stage:adult stage = 0:2:6)
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matrix
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matrix
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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malfunction
in HEK-293 cells, RNA inter ference (RNAi) directed against AK4 inhibits proliferation and promotes death. RNAi directed against AK4 inhibits cell proliferation and causes death in both cell types, HEK-293 and Hep-G2, although cell cycle parameters are affected only in Hep-G2 cells. Reductions of AK4 levels are always associated with cell death
physiological function
adenylate kinase isozyme 4 belongs to a family of nucleotide monophosphate kinases involved in energy metabolism. Enzyme AK4 play a role in protection from stress. In HEK-293 cells, hypoxia increases AK4 expression but does not affect proliferation or viability. Hep-G2 cells show much higher AK4 levels, which decrease under hypoxia along with markedly reduced cell proliferation and increased cell death. AK4-mediated stress protection is not limited to one particular death scenario
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26700
Q964H2
calculated without His-tag
30000
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x * 30000, SDS-PAGE
additional information
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additional information
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additional information
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amino acid sequence
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x-ray diffraction analysis
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crystallized in open conformation and co-crystallized with diguanosine pentaphosphate in closed conformation
crystallized without co-factor as a monomeric protein
sitting drop vapor diffusion method, using 1.9-2.1 M ammonium sulfate, 0.1 M Tris-HCl pH 8.0
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additional information
expression of RNA interference directed against AK4
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0
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5 min, 2 mg protein/ml, stable in 0.1 N HCl
30 - 65
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soluble isoenzyme Adk2p (long), 66% of the maximum activity at 30°C, about 16% activity at 65°C
35
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soluble isoenzyme Adk2p (short) inactivated
40
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5 min, 2 mg protein/ml, in 0.1 N HCl, 70% loss of activity
95
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5 min, 95% inactivation at pH 7.4, 0.15 M imidazole buffer
additional information
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35% ammonium sulfate, AMP or other substrates enhance thermal stability
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ammonium sulfate or substrates enhance stability
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freeze-thawing, dilutions, or low ionic strength decreases activity rapidly
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significant portion of soluble isoenzyme Adk2p (long) remains undigested at 0.02 mg/ml trypsin
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soluble isoenzyme Adk2p (long) is completely inactivated at 5.6 M urea
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soluble isoenzyme Adk2p (short) is completely degraded at 0.002 mg/ml trypsin
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soluble isoenzyme Adk2p (short) is completely inactivated at 1.6 M urea
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stability increases during purification
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-20°C to 4°C, a few weeks
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0°C, partially purified preparation, several weeks
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room temperature, 1 week
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HisTrap column chromatography and Superdex 200 gel filtration
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Ni2+-affinity chromatography
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expressed in Escherichia coli
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expressed in Escherichia coli BL21 (DE3) Rosetta 2 cells
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expressed in soluble form in Escherichia coli by fusion to an RNA-interacting domain derived from human Lys-tRNA synthetase
expression in Escherichia coli
expression in Escherichia coli strain M15
Q964H2
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HepG2 cells show high AK4 levels, which decrease under hypoxia
in HEK293 cells, hypoxia increases AK4 expression
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diagnostics
CsAK3, either alone or in combination with other antigens, can be used for improving the clinical diagnosis of clonorchiasis
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Albrecht, G.J.
Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria
Biochemistry
9
2462-2470
1970
Bos taurus
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Pai, E.F.; Schulz, G.E.; Tomasselli, A.G.; Noda, L.H.
Preliminary X-ray studies on the GTP: AMP phosphotransferase from beef heart mitochondria
J. Mol. Biol.
164
347-350
1983
Bos taurus
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Wieland, B.; Tomasselli, A.G.; Noda, L.H.; Frank, R.; Schulz, G.E.
The amino acid sequence of GTP:AMP phosphotransferase from beef-heart mitochondria. Extensive homology with cytosolic adenylate kinase
Eur. J. Biochem.
143
331-339
1984
Bos taurus
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Diederichs, K.; Schulz, G.E.
Three-dimensional structure of the complex between the mitochondrial matrix adenylate kinase and its substrate AMP
Biochemistry
29
8138-8144
1990
Bos taurus
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Chiga, M.; Rogers, A.E.; Plaut, G.W.E.
Nucleotide transphosphorylases from liver
J. Biol. Chem.
236
1800-1805
1961
Sus scrofa
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Xu, G.; O'Connell, P.; Stevens, J.; White, R.
Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene
Genomics
13
537-542
1992
Homo sapiens
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Heppel, L.A.; Strominger, J.L.; Maxwell, E.S.
Nucleoside monophosphate kinase, II. Transphosphorylation between adenosine monophophate and nucleoside triphosphates
Biochim. Biophys. Acta
32
422-430
1959
Bos taurus
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Gu, Y.; Gordon, D.M.; Amutha, B.; Pain, D.
A GTP:AMP phosphotransferase, Adk2p, in Saccharomyces cerevisiae. Role of the C terminus in protein folding/stabilization, thermal tolerance, and enzymatic activity
J. Biol. Chem.
280
18604-18609
2005
Saccharomyces cerevisiae
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Ulschmid, J.K.; Rahlfs, S.; Schirmer, R.H.; Becker, K.
Adenylate kinase and GTP:AMP phosphotransferase of the malarial parasite Plasmodium falciparum. Central players in cellular energy metabolism
Mol. Biochem. Parasitol.
136
211-220
2004
Plasmodium falciparum (Q964H2), Plasmodium falciparum
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Yang, G.; Yu, X.; Wu, Z.; Xu, J.; Song, L.; Zhang, H.; Hu, X.; Zheng, N.; Guo, L.; Dai, J.; Ji, C.; Gu, S.; Ying, K.
Molecular cloning and characterization of a novel adenylate kinase 3 gene from Clonorchis sinensis
Parasitol. Res.
95
406-412
2005
Clonorchis sinensis (Q564A6), Clonorchis sinensis
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Law, A.; Lescar, J.; Hao, Q.; Kotaka, M.
Expression, purification, crystallization and preliminary X-ray analysis of Plasmodium falciparum GTP:AMP phosphotransferase
Acta Crystallogr. Sect. F
68
671-674
2012
Plasmodium falciparum
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Ma, J.; Rahlfs, S.; Jortzik, E.; Schirmer, R.H.; Przyborski, J.M.; Becker, K.
Subcellular localization of adenylate kinases in Plasmodium falciparum
FEBS Lett.
586
3037-3043
2012
Plasmodium falciparum
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Kong, F.; Binas, B.; Moon, J.H.; Kang, S.S.; Kim, H.J.
Differential expression of adenylate kinase 4 in the context of disparate stress response strategies of HEK293 and HepG2 cells
Arch. Biochem. Biophys.
533
11-17
2013
Homo sapiens (P27144)
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Kwon, S.B.; Kim, P.; Woo, H.S.; Kim, T.Y.; Kim, J.Y.; Lee, H.M.; Jang, Y.S.; Kim, E.M.; Yong, T.S.; Seong, B.L.
Recombinant adenylate kinase 3 from liver fluke Clonorchis sinensis for histochemical analysis and serodiagnosis of clonorchiasis
Parasitology
145
1531-1539
2018
Clonorchis sinensis (Q564A6), Clonorchis sinensis
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Ionescu, M.I.
Adenylate kinase a ubiquitous enzyme correlated with medical conditions
Protein J.
38
120-133
2019
Homo sapiens (P27144), Homo sapiens (Q9UIJ7)
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