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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Homo sapiens and UniProt Accession Q9Y3D8

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EC Tree
IUBMB Comments
Inorganic triphosphate can also act as donor.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9Y3D8
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphotransferase, adenylate kinase, myokinase, adenylate kinase 1, adenylate kinase 2, nonstructural protein 4b, cinap, adenylokinase, structural maintenance of chromosome protein, atp:amp phosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-AMP-kinase
-
-
-
0
ABC adenylate kinase
247
-
adenylate kinase 1
247
isoform
adenylate kinase 2
247
isoform
adenylate kinase 4
290858
-
adenylate kinase 5
290854
isozyme, human AK5 has two separate functional domains both having enzymatic activity
adenylate kinase 9
247
-
adenylic kinase
-
-
-
0
adenylokinase
-
-
-
0
ADK
247
-
AK1
247
isoform
AK2
247
isoform
AK5
290854
isozyme
AK5p1
290854
domain of adenylate kinase 5, human AK5 has two separate functional domains both having enzymatic activity
AK5p2
290854
domain of adenylate kinase 5, human AK5 has two separate functional domains both having enzymatic activity
AK6
298950
-
AK9
247
-
CFTR
281531
-
CINAP
298950
-
coilin interacting nuclear ATPase protein
298950
-
cystic fibrosis transmembrane conductance regulator
281531
-
kinase, adenylate (phosphorylating)
-
-
-
0
kinase, myo- (phosphorylating)
-
-
-
0
myokinase
-
-
-
0
phosphotransferase
298950
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + AMP = 2 ADP
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
0
SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-02-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
2 ADP
ATP + AMP
show the reaction diagram
-
-
-
-
?
adenosine 5'-(3-thio)triphosphate + AMP
adenosine 5'-diphosphate + adenosine 5'-(3-thio)diphosphate
show the reaction diagram
-
muscle: reaction at 97% the rate of ATP, liver mitochondria: reaction at 70% the rate of ATP
-
-
?
ADP
AMP + ATP
show the reaction diagram
-
-
-
-
r
ADP
ATP + AMP
show the reaction diagram
-
-
-
-
r
ADP + ADP
?
show the reaction diagram
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
AMP + ATP
ADP
show the reaction diagram
-
-
-
?
AMP + H2O
ADP + phosphate
show the reaction diagram
GMP can not be substituted for the AMP substrate
-
-
r
ATP + adenosine 5'-thiophosphate
?
show the reaction diagram
-
muscle: reaction at 56% the rate of AMP, liver mitochondria: reaction at 95% the rate of AMP
-
-
?
ATP + AMP
2 ADP
show the reaction diagram
ATP + AMP
ADP
show the reaction diagram
ATP + AMP
ADP + ADP
show the reaction diagram
ATP + AMP-3'-diphosphate
?
show the reaction diagram
-
muscle: reaction at 57% the rate of AMP, liver mitochondria: reaction at 86% the rate of AMP
-
-
?
ATP + CMP
ADP + ?
show the reaction diagram
-
reaction at 1% the rate of AMP
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
ATP + dAMP
ADP + dADP
show the reaction diagram
ATP + dCMP
ADP + dCDP
show the reaction diagram
adenylate kinase 5 domain AK5p1, the relative efficiency of dCMP is about 15% compared to AMP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
r
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at about 3% the rate of ATP
-
-
?
CTP + AMP
CDP + ADP
show the reaction diagram
-
-
-
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
dCTP + AMP
dCDP + ADP
show the reaction diagram
-
-
-
-
?
dGTP + AMP
dGDP + ADP
show the reaction diagram
-
-
-
-
?
dTTP + AMP
dTDP + ADP
show the reaction diagram
-
-
-
-
?
GTP + AMP
GDP + ADP
show the reaction diagram
ITP + AMP
IDP + ADP
show the reaction diagram
-
not ATP/IMP
-
-
?
UTP + AMP
UDP + ADP
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + ADP
?
show the reaction diagram
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
Ba2+
-
forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Mn2+
-
forms complex with di- or trinucleotide
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
P1,P5-diadenosine 5'-pentaphosphate
adenylate kinase-specific inhibitor, potent inhibitor of CINAP
5,5'-dithiobis(2-nitrobenzoic acid)
adenosine 5'-pentaphosphate
-
inhibits the RAD50 phosphoryl transfer reaction but not ATP hydrolysis
D-glucose
-
elevated concentrations of glucose inhibit cytosolic isoform AK1 expression. Inhibition of adenylate kinase increases the ATP/ADP ratio in the microenvironment of the K/ATP channel promoting channel closure and insulin secretion
diadenosine polyphosphate
inhibits adenylate kinase activity of the nucleotide-binding domains 1 and 2 of CFTR
-
F-
-
not
homologous antibodies
-
-
-
iodoacetate
-
temperature-dependent
Methylmercury nitrate
-
-
p-hydroxymercuribenzoate
-
-
P1,P4-bis(adenosine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P4-di(adenosine-5') tetraphosphate
-
Ap4A
P1,P4-di(uridine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P5-di(adenosine-5') pentaphosphate
-
Ap5A, interacts simultaneously with an AMP-binding site and ATP-binding site 2
P1,P5-di(adenosine-5')pentaphosphate
suramin
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
uridine adenosine tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
additional information
-
not inhibitory: p-chloromercuribenzoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
induction of cellular ATP production via adenylate kinase resulting in regulation of ADP-dependent endocytosis of high-density lipoprotein
AMP
-
adenylate kinase activation by ATP and AMP stimulates K/ATP channel activity and this stimulation is abolished by adenylate kinase inhibitors
ATP
-
adenylate kinase activation by ATP and AMP stimulates K/ATP channel activity and this stimulation is abolished by adenylate kinase inhibitors
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045 - 0.093
ATP
0.15
2 ADP
-
ADP in form of MgADP-
-
0.05 - 0.35
ADP
0.09 - 0.092
ADP3-
0.0014 - 1.7
AMP
0.044 - 1.03
ATP
0.507 - 2
dAMP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037 - 0.0063
ATP
783
ADP
-
-
0.16 - 842.3
AMP
0.1 - 879.5
ATP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
39000 - 140000
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00002703
P1,P5-diadenosine 5'-pentaphosphate
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.011
mutant enzyme CINAP H79G, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.018
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.6
nucleotide-binding domain 2 of wild type, with ATP
1
nucleotide-binding domain 1 of wild type, with ADP
1480
-
allelozyme AK1*1
1600 - 1700
-
muscle, 30°C, pH 8.1
2000
wild-type, 37°C
225 - 250
-
liver, 30°C, pH 8.1
280
-
30°C, pH 7.4
420
-
allelozyme AK1*2
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
AMP + ATP
7.5
-
assay at
7.9
-
ADP + ADP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.2
-
about half-maximal activity at pH 6.5 and 8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
additional information
-
effect of temperature on initial velocity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
vascular endothelial cells
Manually annotated by BRENDA team
-
in primary culture
Manually annotated by BRENDA team
-
adenylate kinase 2 is specifically expressed in the stria vascularis region of the inner ear
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
cytosolic isoforms AK1 and AK5 are expressed in human islets and INS-1 cells. Elevated concentrations of glucose inhibit AK1 expression
Manually annotated by BRENDA team
-
moderate expression
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
moderate expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
extracellular activity is less than 1% of total activity and due to leaking from leaving cells or to dying cells
-
Manually annotated by BRENDA team
-
extracellular activity is less than 1% of total activity and due to leaking from leaving cells or to dying cells
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
adenylate kinase 4 is a unique member of the adenylate kinases family which shows no enzymatic activity in vitro
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KAD6_HUMAN
172
0
20061
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21300
21500
21635
x * 22000, SDS-PAGE, x * 21635, calculated
21700
22000
22500
-
isozyme AKalpha, gel filtration
22600
-
titration of 2 SH-groups
23000
23400
-
1 * 23400, isozyme AKalpha, sedimentation equilibrium in 6 M guanidine hydrochloride
25000
-
SDS-PAGE
25200
-
liver, sedimentation equilibrium
25400
-
sedimentation equilibrium
25600
-
x * 25600, SDS-PAGE
26000
-
adenylate kinase 2, SDS-PAGE
26349
-
1 * 26349, calculated from amino acid analysis
26350
-
calculated from amino acid analysis
26500
-
1 * 26500, SDS-PAGE
48500
-
x * 48500, calculated from amino acid sequence
53000
SDS-PAGE, fused with the GST tag the recombinant protein has a size of about 53000 Da
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Western blot analysis, SDS-PAGE
monomer
additional information
-
cytosolic isoform AK1 immunoprecipitates with the Kir6.2 subunit of K/ATP channel
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ADP, dADP, and Mg2+ADP-PO43-, hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 1.5 M Li2SO4, 0.2 M NaCl, 0.5 mM dithiothreitol, and 25 mM MgCl2
mutant enzyme L171P, hanging drop vapor diffusion method, 4°C under conditions of 1.22-1.28 M (NH4)2SO4 and 0.1 M Tris-HCl, pH 8.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H79G
the mutation affects both adenylate kinase (enzymatic efficiency (kcat/Km) is reduced by 72% relative to the wild type enzyme) and ATPase catalytic efficiency and induces homodimer formation
C40V
-
the mutation is associated with reticular dysgenesis
D140del
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 30% residual adenylate kinase activity
D165G
-
the mutation is associated with reticular dysgenesis
E9X
-
the mutation is associated with reticular dysgenesis
G40R
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 25% residual adenylate kinase activity
K233X
-
the mutation is associated with reticular dysgenesis
K4G
when the amino acid residue is mutated, the protein is imported in mitochondria
K4G/R7G
when both amino acid residues are mutated simultaneously the protein remains in the cytosol
L1254A
-
mutant in cystic fibrosis transmembrane conductance regulator. Cystic fibrosis transmembrane conductance regulator shows adenylate kinase activity in the presence of ATP plus physiologic concentrations of AMP or ADP. P1,P5-di(adenosine-5') pentaphosphate increases the activity of the mutant. The mutation increases the EC50 for ATP by more than 10-fold and reduces channel activity by prolonging the closed state. P1,P5-di(adenosine-5') pentaphosphate changes the relationship between ATP concentration and current. At submaximal ATP concentrations, P1,P5-di(adenosine-5') pentaphosphate stimulates current by stabilizing the channel open state
L171P
the mutation dramatically changes the orientation of the LID domain, which can be described as a twisted and closed conformation in contrast to the open and closed conformations in other adenylate kinases
L183X
-
the mutation is associated with reticular dysgenesis
M1V
-
the mutation is associated with reticular dysgenesis
R103W
-
the mutation is associated with reticular dysgenesis
R128W
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 44% residual adenylate kinase activity
R186C
-
the mutation is associated with reticular dysgenesis
R7G
when the amino acid residue is mutated, the protein is imported in mitochondria
S1202R
-
mutation of RAD50 signature motif, 10-50% of wild-type activity in formation of ADP, formation of ATP is not affected
S231D
-
the mutation is associated with reticular dysgenesis
Y152T
-
the mutation is associated with reticular dysgenesis
Y164C
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 0% residual adenylate kinase activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.5
-
1 h, at 0°C, quite stable
642559
2
-
1 h, at 0°C, quite stable
642559
5 - 6
-
70% loss of activity at pH 5 in 50 mM acetate buffer and 30% loss of activity at pH 6 in phosphate buffer, at 4°C overnight
642589
6 - 8
-
10 min, at 90°C, in 10 mM phosphate buffer, pH 7, 0.1 M KCl, DTT, Triton X-100, +/- EDTA, 10% loss of activity within 10 min
642567
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
stable for 3 h
50
-
enzyme type 2: in 10 mM sodium citrate buffer, pH 6, t1/2: 5 min, enzyme type 1: t1/2: 31 min
90
-
in 10 mM phosphate buffer, pH 7, 0.1 M KCl, 0.02% Triton X-100, 2 mM DTT, +/- EDTA, t1/2: 10 min, with more than 0.2 M KCl: 10-20% loss of activity within 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at low dithioerythritol concentrations enzyme tends to aggregate
-
bovine serum albumin, 1 mg/ml, stabilizes dilute enzyme solutions
-
diadenosine pentaphosphate, i.e. AP5A, stabilizes during preparative electrophoresis
-
in crude haemolysates type 1 enzyme is more stable than type 2, DTT or bovine serum albumin stabilizes
-
low ionic strength inactivates
-
stable to dialysis in the presence of 4 mM dithioerythritol
-
Stable to freeze-thawing
-
Triton X-100, EDTA, dithiothreitol and electrolyte protect enzyme in dilute solution and against denaturation by heat or extreme pH-values
-
unstable in dilute solution
-
unstable in dilute solution, 0.2 mg/ml, dithioerythritol, and bovine serum albumin stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several weeks
-
0°C, a few days stable, after which activity drops to 70%, this lower specific activity can be maintained at -20°C in ammonium sulfate solution for a prolonged period
-
3°C, 5-10% loss within 1 month
-
4°C, in distilled water, 6 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GSTrap 4B column chromatography and Superdex 75 gel filtration
2 allelozymes: AK1*1 and AK1*2
-
2 isozymes, partial
-
and their multiple forms
-
glutathione-Sepharose column chromatography
muscle
-
nucleotide-binding domain 1 and 2, purified to homogeneity under denaturing conditions
predominant form AKalpha (major form of AK-1 isozymes)
-
separable by electrophoresis, not by isoelectric focusing
-
Sepharose column chromatography and Superdex 75 gel filtration
TALON metal affinity resin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834(DE3)pLysS cells
cloned into vector pET28b and expressed in Escherichia coli BL21DE3pLys cells
cytosolic isoforms AK1 and AK5 are expressed in human islets and INS-1 cells. Elevated concentrations of glucose inhibit AK1 expression
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
expression in HeLa cell
-
wild-type and mutant CFTR are transiently expressed in HeLa cell membranes a double vaccinia virus/T7 RNA polymerase system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
adenylate kinase activity is significantly higher after extremely low frequency electromagnetic field treatment with an increase of about 102% compared to control cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noda, L.
Adenylate kinase
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
8
279-305
1973
Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Citrus limon, Blattidae, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mus musculus, Physarum polycephalum, Rattus norvegicus, Sus scrofa, Thiobacillus denitrificans, Triticum aestivum
-
Manually annotated by BRENDA team
Hamada, M.; Sumida, M.; Okuda, H.; Watanabe, T.; Nojima, M.; Kuby, S.A.
Adenosine triphosphate-adenosine-5-monophosphate phosphotransferase from normal human liver mitochondria. Isolation, chemical properties, and immunochemical comparison with Duchenne dystrophic serum aberrant adenylate kinase
J. Biol. Chem.
257
13120-13128
1982
Homo sapiens
Manually annotated by BRENDA team
Kuby, S.A.; Fleming, G.; Frischat, A.; Cress, M.C.; Hamada, M.
Studies on adenosine triphosphate transphosphorylases. Human isoenzymes of adenylate kinase: isolation and physicochemical comparison of the crystalline human ATP-AMP transphosphorylases from muscle and liver
J. Biol. Chem.
258
1901-1907
1983
Bos taurus, Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Luz, C.M.; König, I.; Schirmer, R.H.; Frank, R.
Human cytosolic adenylate kinase allelozymes; purification and characterization
Biochim. Biophys. Acta
1038
80-84
1990
Homo sapiens
Manually annotated by BRENDA team
Brownson, C.; Spencer, N.
Partial purification and properties of the two common inherited forms of human erythrocyte adenylate kinase
Biochem. J.
130
797-803
1972
Homo sapiens
Manually annotated by BRENDA team
Thuma, E.; Schirmer, R.H.; Schirmer, I.
Preparation and characterization of a crystalline human ATP:AMP phosphotransferase
Biochim. Biophys. Acta
268
81-91
1972
Homo sapiens
Manually annotated by BRENDA team
Schirmer, R.H.; Thuma, E.
Sensitivity of adenylate kinase isozymes from normal and dystrophic human muscle to sulfhydryl reagents
Biochim. Biophys. Acta
268
92-97
1972
Homo sapiens
Manually annotated by BRENDA team
Khoo, J.C.; Russell, P.J.
Isoenzymes of adenylate kinase in human tissue
Biochim. Biophys. Acta
268
98-101
1972
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Tsuboi, K.K.; Chervenka, C.H.
Adenylate kinase of human erythrocyte. Isolation and properties of the predominant inherited form
J. Biol. Chem.
250
132-140
1975
Homo sapiens
Manually annotated by BRENDA team
Terai, H.
Adenylate kinase from Pseudomonas denitrificans. I. Purification and antiserum inhibition
J. Biochem.
75
1027-1036
1974
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Pseudomonas denitrificans (nomen rejiciendum), Rattus norvegicus
Manually annotated by BRENDA team
Tsuboi, K.K.
AMP (dAMP) kinase from human erythrocytes
Methods Enzymol.
51
467-473
1978
Homo sapiens
Manually annotated by BRENDA team
Lee, Y.; Kim, J.W.; Lee, S.M.; Kim, H.J.; Lee, K.S.; Park, C.; Choe, I.S.
Cloning and expression of human adenylate kinase 2 isoenzymes: differential expression of adenylate kinase 1 and 2 in human muscle tissues
J. Biochem.
123
47-54
1998
Homo sapiens
Manually annotated by BRENDA team
Yan, H.; Tsai, M.D.
Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity
Adv. Enzymol. Relat. Areas Mol. Biol.
73
103-134
1999
Bacillus subtilis, Bos taurus, Oryctolagus cuniculus, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Ren, H.; Wang, L.; Bennett, M.; Liang, Y.; Zheng, X.; Lu, F.; Li, L.; Nan, J.; Luo, M.; Eriksson, S.; Zhang, C.; Su, X.D.
The crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus
Proc. Natl. Acad. Sci. USA
102
303-308
2005
Homo sapiens
Manually annotated by BRENDA team
Fabre, A.C.; Vantourout, P.; Champagne, E.; Terce, F.; Rolland, C.; Perret, B.; Collet, X.; Barbaras, R.; Martinez, L.O.
Cell surface adenylate kinase activity regulates the F(1)-ATPase/P2Y (13)-mediated HDL endocytosis pathway on human hepatocytes
Cell. Mol. Life Sci.
63
2829-2837
2006
Homo sapiens
Manually annotated by BRENDA team
Abrusci, P.; Chiarelli, L.R.; Galizzi, A.; Fermo, E.; Bianchi, P.; Zanella, A.; Valentini, G.
Erythrocyte adenylate kinase deficiency: characterization of recombinant mutant forms and relationship with nonspherocytic hemolytic anemia
Exp. Hematol.
35
1182-1189
2007
Homo sapiens (P00568), Homo sapiens
Manually annotated by BRENDA team
Quillen, E.E.; Haslam, G.C.; Samra, H.S.; Amani-Taleshi, D.; Knight, J.A.; Wyatt, D.E.; Bishop, S.C.; Colvert, K.K.; Richter, M.L.; Kitos, P.A.
Ectoadenylate kinase and plasma membrane ATP synthase activities of human vascular endothelial cells
J. Biol. Chem.
281
20728-20737
2006
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Gross, C.H.; Abdul-Manan, N.; Fulghum, J.; Lippke, J.; Liu, X.; Prabhakar, P.; Brennan, D.; Willis, M.S.; Faerman, C.; Connelly, P.; Raybuck, S.; Moore, J.
Nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator, an ABC transporter, catalyze adenylate kinase activity but not ATP hydrolysis
J. Biol. Chem.
281
4058-4068
2006
Homo sapiens (P13569), Homo sapiens, Mus musculus (P26361), Mus musculus
Manually annotated by BRENDA team
Bhaskara, V.; Dupre, A.; Lengsfeld, B.; Hopkins, B.B.; Chan, A.; Lee, J.H.; Zhang, X.; Gautier, J.; Zakian, V.; Paull, T.T.
Rad50 adenylate kinase activity regulates DNA tethering by Mre11/Rad50 complexes
Mol. Cell
25
647-661
2007
Saccharomyces cerevisiae, Homo sapiens, Pyrococcus furiosus, Xenopus laevis
Manually annotated by BRENDA team
Stanojevic, V.; Habener, J.F.; Holz, G.G.; Leech, C.A.
Cytosolic adenylate kinases regulate K-ATP channel activity in human beta-cells
Biochem. Biophys. Res. Commun.
368
614-619
2008
Homo sapiens
Manually annotated by BRENDA team
Dong, Q.; Randak, C.O.; Welsh, M.J.
A mutation in CFTR modifies the effects of the adenylate kinase inhibitor Ap5A on channel gating
Biophys. J.
95
5178-85
2008
Homo sapiens
Manually annotated by BRENDA team
Yegutkin, G.G.; Jankowski, J.; Jalkanen, S.; Guenthner, T.; Zidek, W.; Jankowski, V.
Dinucleotide polyphosphates contribute to purinergic signalling via inhibition of adenylate kinase activity
Biosci. Rep.
28
189-194
2008
Homo sapiens
Manually annotated by BRENDA team
Tuezuen, E.; Rossi, J.E.; Karner, S.F.; Centurion, A.F.; Dalmau, J.
Adenylate kinase 5 autoimmunity in treatment refractory limbic encephalitis
J. Neuroimmunol.
186
177-180
2007
Homo sapiens
Manually annotated by BRENDA team
Liu, R.; Xu, H.; Wei, Z.; Wang, Y.; Lin, Y.; Gong, W.
Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion
Biochem. Biophys. Res. Commun.
379
92-97
2009
Homo sapiens (P27144), Homo sapiens
Manually annotated by BRENDA team
Solaroli, N.; Panayiotou, C.; Johansson, M.; Karlsson, A.
Identification of two active functional domains of human adenylate kinase 5
FEBS Lett.
583
2872-2876
2009
Homo sapiens (Q9Y6K8), Homo sapiens
Manually annotated by BRENDA team
Panayiotou, C.; Solaroli, N.; Johansson, M.; Karlsson, A.
Evidence of an intact N-terminal translocation sequence of human mitochondrial adenylate kinase 4
Int. J. Biochem. Cell Biol.
42
62-69
2010
Homo sapiens (P27144)
Manually annotated by BRENDA team
Albanese, A.; Battisti, E.; Vannoni, D.; Aceto, E.; Galassi, G.; Giglioni, S.; Tommassini, V.; Giordano, N.
Alterations in adenylate kinase activity in human PBMCs after in vitro exposure to electromagnetic field: comparison between extremely low frequency electromagnetic field (ELF) and therapeutic application of a musically modulated electromagnetic field (TAMMEF)
J. Biomed. Biotechnol.
2009
717941
2009
Homo sapiens
Manually annotated by BRENDA team
Pannicke, U.; Hoenig, M.; Hess, I.; Friesen, C.; Holzmann, K.; Rump, E.M.; Barth, T.F.; Rojewski, M.T.; Schulz, A.; Boehm, T.; Friedrich, W.; Schwarz, K.
Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2
Nat. Genet.
41
101-105
2009
Homo sapiens, Danio rerio (Q1L8L9), Danio rerio
Manually annotated by BRENDA team
Lagresle-Peyrou, C.; Six, E.M.; Picard, C.; Rieux-Laucat, F.; Michel, V.; Ditadi, A.; Demerens-de Chappedelaine, C.; Morillon, E.; Valensi, F.; Simon-Stoos, K.L.; Mullikin, J.C.; Noroski, L.M.; Besse, C.; Wulffraat, N.M.; Ferster, A.; Abecasis, M.M.; Calvo, F.; Petit, C.; Candotti, F.; Abel, L.; Fis, F.i.s.c.
Human adenylate kinase 2 deficiency causes a profound hematopoietic defect associated with sensorineural deafness
Nat. Genet.
41
106-111
2009
Homo sapiens
Manually annotated by BRENDA team
Amiri, M.; Conserva, F.; Panayiotou, C.; Karlsson, A.; Solaroli, N.
The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase
Int. J. Biochem. Cell Biol.
45
925-931
2013
Homo sapiens
Manually annotated by BRENDA team
Drakou, C.E.; Malekkou, A.; Hayes, J.M.; Lederer, C.W.; Leonidas, D.D.; Oikonomakos, N.G.; Lamond, A.I.; Santama, N.; Zographos, S.E.
hCINAP is an atypical mammalian nuclear adenylate kinase with an ATPase motif: structural and functional studies
Proteins
80
206-220
2012
Homo sapiens (Q9Y3D8), Homo sapiens
Manually annotated by BRENDA team
Randak, C.O.; Dong, Q.; Ver Heul, A.R.; Elcock, A.H.; Welsh, M.J.
ATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites
J. Biol. Chem.
288
27692-27701
2013
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Gan, L.; Wang, E.; Wang, J.
Exploring the dynamic functional landscape of adenylate kinase modulated by substrates
J. Chem. Theory Comput.
9
84-95
2013
Geobacillus stearothermophilus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
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