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Information on EC 2.7.4.6 - nucleoside-diphosphate kinase and Organism(s) Homo sapiens

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IUBMB Comments
Many nucleoside diphosphates can act as acceptors, while many ribo- and deoxyribonucleoside triphosphates can act as donors.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
nm23-h1, nucleoside diphosphate kinase, ndp kinase, nm23-h2, ndpk-b, ndpk2, nucleoside diphosphokinase, ndk-1, nucleoside-diphosphate kinase, nucleoside diphosphate kinase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
kinase, nucleoside diphosphate (phosphorylating)
-
-
-
-
NDP kinase A
-
NDPK-D
NM23 metastasis suppressor
-
exhibits Ndk activity
Nm23-H1
nucleoside 5'-diphosphate kinase
-
-
-
-
nucleoside diphosphate (UDP) kinase
-
-
-
-
nucleoside diphosphate kinase
nucleoside diphosphate kinase A
-
nucleoside diphosphate kinase B
nucleoside diphosphate kinase D
-
nucleoside diphosphokinase
-
-
-
-
nucleoside-diphosphate kinase 3
-
nucleotide phosphate kinase
-
-
-
-
UDP kinase
-
-
-
-
uridine diphosphate kinase
-
-
-
-
additional information
-
the enzyme belongs to the nucleoside diphosphate kinase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:nucleoside-diphosphate phosphotransferase
Many nucleoside diphosphates can act as acceptors, while many ribo- and deoxyribonucleoside triphosphates can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-51-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 8-bromo-IDP
ADP + ?
show the reaction diagram
ATP + CDP
ADP + CTP
show the reaction diagram
-
-
-
-
?
ATP + dTDP
ADP + dTTP
show the reaction diagram
-
-
-
?
ATP + GDP
ADP + GTP
show the reaction diagram
ATP + NDP
ADP + NTP
show the reaction diagram
ATP + TDP
ADP + TTP
show the reaction diagram
gamma-S-ATP + GDP
ADP + gamma-S-GTP
show the reaction diagram
-
poor substrate
-
-
?
gamma-S-GTP + GDP
GDP + gamma-S-GTP
show the reaction diagram
-
poor substrate
-
-
?
GTP + CDP
GDP + CTP
show the reaction diagram
-
-
-
-
?
GTP + dGDP
GDP + dGTP
show the reaction diagram
-
-
-
-
?
GTP + dTDP
GDP + dTTP
show the reaction diagram
-
-
-
-
?
NDP + NTP
NTP + NDP
show the reaction diagram
NTP + nucleoside diphosphate
NDP + NTP
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
ATP + GDP
ADP + GTP
show the reaction diagram
-
-
-
-
?
ATP + NDP
ADP + NTP
show the reaction diagram
ATP + TDP
ADP + TTP
show the reaction diagram
-
-
-
r
NDP + NTP
NTP + NDP
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
requirement, about half as effective as Mg2+, Mn2+ or Co2+, pI 7.3-enzyme variant
Zn2+
-
not
additional information
-
no activation by Cu2+ or monovalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-bromo-IDP
-
in excess
ellagic acid
-
inhibits NDPK and suppresses MDA-MB-435S cell growth
epigallocatechin gallate
-
EGCG, inhibits NDPK and suppresses MDA-MB-435S cell growth
GMP
-
erythrocytic kinase, kinetics
p-chloromercuribenzoate
theophylline
-
-
additional information
-
no inhibition by papaverine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
forskolin
forskolin enhances NDPK-B interaction with CFTR 3fold in 16HBE14o- cells
additional information
-
nucleoside triphosphate, especially GTP, promotes the dynamic self-assembly of isozyme NDPKB into ordered 20-25 nm diameter filaments in vitro
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033 - 0.06
8-bromo-IDP
0.024
ADP
-
cosubstrate GTP
0.2 - 0.38
ATP
-
cosubstrate dTDP, two different assays
0.21 - 0.39
dTDP
-
cosubstrate ATP, two different assays
0.12
GTP
-
cosubstrate ADP
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.003
ellagic acid
Homo sapiens
-
-
0.008 - 0.01
epigallocatechin gallate
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
550
-
isozyme A6, 25°C
740
-
isozyme B6, 25°C
additional information
-
specific activities of a variety of animals, plants and microorganisms
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
-
7.2
-
assembly assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assembly assay at
additional information
-
temperature-dependence of NDP kinases
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression
Manually annotated by BRENDA team
intermediate expression
Manually annotated by BRENDA team
intermediate expression
Manually annotated by BRENDA team
in hepatocarcinoma derived cell lines, NME4 expression is lower in cell lines with high metastatic potential
Manually annotated by BRENDA team
intermediate expression
Manually annotated by BRENDA team
low expression
Manually annotated by BRENDA team
intermediate expression
Manually annotated by BRENDA team
-
isoforms A,B in the ratio 1:3
Manually annotated by BRENDA team
highest expression
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
intermediate expression
Manually annotated by BRENDA team
low expression
Manually annotated by BRENDA team
additional information
HeLa cells are naturally almost devoid of NDPK-D
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted
-
Manually annotated by BRENDA team
structural basis of NDPK-D/mitochondrial membrane interactions via binding of cardiolipin, overview
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KAD4_HUMAN
223
0
25268
Swiss-Prot
Mitochondrion (Reliability: 4)
KAD5_HUMAN
562
0
63333
Swiss-Prot
other Location (Reliability: 1)
KCY_HUMAN
196
0
22222
Swiss-Prot
other Location (Reliability: 5)
NDK3_HUMAN
169
0
19015
Swiss-Prot
Secretory Pathway (Reliability: 2)
NDK6_HUMAN
186
0
21142
Swiss-Prot
other Location (Reliability: 5)
NDK7_HUMAN
376
0
42492
Swiss-Prot
other Location (Reliability: 1)
KAD7_HUMAN
723
0
82658
Swiss-Prot
other Location (Reliability: 1)
KAD8_HUMAN
479
0
54926
Swiss-Prot
other Location (Reliability: 1)
KAD9_HUMAN
1911
0
221413
Swiss-Prot
other Location (Reliability: 1)
NDK8_HUMAN
137
0
15529
Swiss-Prot
other Location (Reliability: 4)
NDKA_HUMAN
152
0
17149
Swiss-Prot
other Location (Reliability: 2)
NDKB_HUMAN
152
0
17298
Swiss-Prot
other Location (Reliability: 2)
CMPK2_HUMAN
449
0
49448
Swiss-Prot
Mitochondrion (Reliability: 1)
KAD1_HUMAN
194
0
21635
Swiss-Prot
other Location (Reliability: 1)
NDKM_HUMAN
187
0
20659
Swiss-Prot
Mitochondrion (Reliability: 2)
Q8N291_HUMAN
241
0
27035
TrEMBL
other Location (Reliability: 1)
H0YID2_HUMAN
51
0
5832
TrEMBL
other Location (Reliability: 2)
A0A384MTW7_HUMAN
152
0
17149
TrEMBL
other Location (Reliability: 2)
F8VZG5_HUMAN
162
0
17499
TrEMBL
other Location (Reliability: 2)
B4DXC8_HUMAN
339
0
38204
TrEMBL
other Location (Reliability: 1)
A0A075B7F5_HUMAN
137
0
16095
TrEMBL
other Location (Reliability: 1)
A0A2R8Y7V2_HUMAN
114
0
12493
TrEMBL
other Location (Reliability: 5)
Q9NUF9_HUMAN
153
0
17296
TrEMBL
other Location (Reliability: 5)
F8VY04_HUMAN
190
0
21226
TrEMBL
other Location (Reliability: 2)
F8VS11_HUMAN
171
0
19781
TrEMBL
other Location (Reliability: 2)
B4DLK2_HUMAN
122
0
13098
TrEMBL
other Location (Reliability: 2)
A0A5F9ZHP2_HUMAN
162
0
17723
TrEMBL
other Location (Reliability: 2)
A0A024R8Z7_HUMAN
340
0
38187
TrEMBL
other Location (Reliability: 3)
Q53EY8_HUMAN
194
0
21619
TrEMBL
other Location (Reliability: 1)
A0A2R8Y547_HUMAN
88
0
9530
TrEMBL
Mitochondrion (Reliability: 3)
A0A5K1VW67_HUMAN
197
0
22090
TrEMBL
other Location (Reliability: 2)
B4DDL4_HUMAN
181
0
20559
TrEMBL
Mitochondrion (Reliability: 3)
H7C505_HUMAN
218
0
25363
TrEMBL
other Location (Reliability: 1)
A0A384N647_HUMAN
223
0
25252
TrEMBL
Mitochondrion (Reliability: 3)
F2Z2X0_HUMAN
233
0
25460
TrEMBL
Mitochondrion (Reliability: 2)
E9PPU7_HUMAN
259
0
29992
TrEMBL
other Location (Reliability: 1)
C9J9V6_HUMAN
174
0
20061
TrEMBL
other Location (Reliability: 5)
E9PQQ8_HUMAN
176
0
19992
TrEMBL
other Location (Reliability: 1)
E9PIS7_HUMAN
77
0
8731
TrEMBL
other Location (Reliability: 4)
Q4TT34_HUMAN
195
0
21522
TrEMBL
Mitochondrion (Reliability: 1)
Q5T9B7_HUMAN
210
0
23411
TrEMBL
other Location (Reliability: 2)
B4DFW6_HUMAN
169
0
19102
TrEMBL
Mitochondrion (Reliability: 3)
J3KP89_HUMAN
736
0
84871
TrEMBL
other Location (Reliability: 1)
A0A494BXC7_HUMAN
179
0
20180
TrEMBL
Mitochondrion (Reliability: 4)
Q6FHN3_HUMAN
152
0
17298
TrEMBL
other Location (Reliability: 2)
Q6FGX9_HUMAN
194
0
21635
TrEMBL
other Location (Reliability: 1)
A0A0C4DG91_HUMAN
194
0
22003
TrEMBL
other Location (Reliability: 4)
C9JQB1_HUMAN
141
0
16188
TrEMBL
other Location (Reliability: 3)
G3V213_HUMAN
133
0
14325
TrEMBL
other Location (Reliability: 2)
H7C517_HUMAN
749
0
87337
TrEMBL
other Location (Reliability: 1)
K4Q5R3_HUMAN
39
0
4653
TrEMBL
other Location (Reliability: 2)
Q5T0D2_HUMAN
169
0
18979
TrEMBL
Mitochondrion (Reliability: 5)
E9PPM3_HUMAN
227
0
26495
TrEMBL
other Location (Reliability: 3)
H3BPR2_HUMAN
85
0
9283
TrEMBL
Secretory Pathway (Reliability: 5)
H0YCD1_HUMAN
192
0
22828
TrEMBL
other Location (Reliability: 1)
A0A087WVT9_HUMAN
153
0
16783
TrEMBL
Mitochondrion (Reliability: 2)
Q32Q12_HUMAN
292
0
32642
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8I5KW96_HUMAN
223
0
25208
TrEMBL
Mitochondrion (Reliability: 4)
B3KWD9_HUMAN
157
0
18178
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
erythrocytic enzyme variant pI 8.3, gel filtration
105000
-
gel filtration
19000
-
x * 19000 + x * 20500, SDS-PAGE
20500
-
x * 19000 + x * 20500, SDS-PAGE
80000
-
erythrocytic enzyme variants pI 5.4 and pI 6.8, gel filtration
80000 - 100000
-
erythrocytic enzyme variants
84000
-
erythrocytic enzyme variants pI 6.3 and pI 7.3, gel filtration
93000
-
erythrocytic enzyme variant pI 5.8, gel filtration
additional information
-
comparison of kinase amino acid sequences
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant H118G/F60W in complex with ADP, Ca2+ and phosphate
-
wild-type and mutant S120G in complex with ADP, no significant changes between wild-type and mutant even in the surroundings of the catalytic His residue
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H118C
-
the mutant of isozyme NDPKB is catalytically inactive
H118G/F60W
-
mutant engineered for following intrinsic fluorescence during substrate binding, crystallization data
H118N/S120G
site-directed mutagenesis, the mutant is inactive and expressed as insoluble protein in inclusion bodies
K135L
-
isoform B, mutation in dimeric interface, defective DNA-binding and reduced stability of enzyme
N69H
-
isoform B, mutation in dimeric interface, defective DNA-binding and reduced stability of enzyme
R34G
-
isoform B, mutation in dimeric interface, defective DNA-binding and reduced stability of enzyme
R90D
site-directed mutagenesis, the mutant does not bind to cardiolipin
S120G
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
3 h, 50% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on Cibacron Red 3B-P-Sepharose
-
marked isoelectric variability with pIs from 5.4 to 8.3
-
native enzyme partially by mitochondrion preparation
Ni-NTA column chromatography
-
recombinant His-tagged wild-type and mutant NDPKB by nickel affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant wild-type and mutant enzymes by anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expression of GST-fusion NM23 protein in Escherichia coli
-
expression of His-tagged wild-type and mutant NDPKB
-
expression of wild-type and mutant enzymes
overview
-
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in human airway cells exposed to hypoxia (3% oxygen) membrane-bound and cytosolic NDPK is inhibited
-
overexpression of NME4 mRNA in several types of tumors
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation of subunit polypeptides A and B generates several isozymes
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lam, S.C.T.; Packham, M.A.
Isolation and kinetic studies of nucleoside diphosphokinase from human platelets and effects of cAMP phosphodiesterase inhibitors
Biochem. Pharmacol.
35
4449-4455
1986
Homo sapiens
Manually annotated by BRENDA team
Presecan, E.; Vonica, A.; Lascu, I.
Nucleoside diphosphate kinase from human erythrocytes: purification, molecular mass and subunit structure
FEBS Lett.
250
629-632
1989
Homo sapiens
Manually annotated by BRENDA team
Gilles, A.M.; Presecan, E.; Vonica, A.; Lascu, I.
Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme
J. Biol. Chem.
266
8784-8789
1991
Homo sapiens
Manually annotated by BRENDA team
Hemmerich, S.; Pecht, I.
Oligomeric structure and autophosphorylation of nucleoside diphosphate kinase from rat mucosal mast cells
Biochemistry
31
4580-4587
1992
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Agarwal, R.P.; Robison, B.; Parks, R.E.
Nucleoside diphosphokinase from human erythrocytes
Methods Enzymol.
51
376-386
1978
Homo sapiens
Manually annotated by BRENDA team
Parks, R.E.; Agarwal, R.P.
Nucleoside diphosphokinases
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
8
307-333
1973
Anguilla rostrata, Avian myeloblastosis virus, Papio sp., Bacillus subtilis, Beta vulgaris subsp. vulgaris, Bos taurus, Saccharomyces cerevisiae, Vicia faba, Canis lupus familiaris, Gallus gallus, Columba livia, Oryctolagus cuniculus, Streptococcus pneumoniae, Escherichia coli, Felis catus, Helianthus tuberosus, Homo sapiens, Hordeum vulgare, Impatiens holstii, Micrococcus luteus, Platyrrhini, Mus musculus, Myxine glutinosa, Phoca vitulina, Pisum sativum, Rattus norvegicus, Saccharomyces pastorianus, Saccharum officinarum, Schistosoma mansoni, Solanum tuberosum, Squalus acanthias, Sus scrofa, Triticum aestivum
-
Manually annotated by BRENDA team
Schaertl, S.; Konrad, M.; Geeves, M.A.
Substrate specificity of human nucleoside-diphosphate kinase revealed by transient kinetic analysis
J. Biol. Chem.
273
5662-5669
1998
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Gallois-Montbrun, S.; Schneider, B.; Veron, M.; Morera, S.; Deville-Bonne, D.; Janin, J.
Nucleotide Binding to Nucleoside Diphosphate Kinases: X-ray Structure of Human NDPK-A in Complex with ADP and Comparison to Protein Kinases
J. Mol. Biol.
332
915-926
2003
Homo sapiens
Manually annotated by BRENDA team
Bourdais, J.; Biondi, R.; Sarfati, S.; Guerreiro, C.; Lascu, I.; Janin, J.; Veron, M.
Cellular phosphorylation of anti-HIV nucleosides. Role of nucleoside diphosphate kinase
J. Biol. Chem.
271
7887-7890
1996
Homo sapiens
Manually annotated by BRENDA team
Kim, S.Y.; Song, E.J.; Chang, K.H.; Kim, E.; Chae, S.K.; Lee, H.; Lee, K.J.
Oligomeric structures determine the biochemical characteristics of human nucleoside diphosphate kinases
J. Biochem. Mol. Biol.
34
355-364
2001
Homo sapiens
-
Manually annotated by BRENDA team
Lacombe, M.L.; Milon, L.; Munier, A.; Mehus, J.G.; Lambeth, D.O.
The human Nm23/nucleoside diphosphate kinases
J. Bioenerg. Biomembr.
32
247-258
2000
Homo sapiens
Manually annotated by BRENDA team
Janin, J.; Deville-Bonne, D.
Nucleoside-diphosphate kinase: structural and kinetic analysis of reaction pathway and phosphohistidine intermediate
Methods Enzymol.
354
118-134
2002
Bos taurus, Dictyostelium discoideum, Drosophila melanogaster, Homo sapiens, Myxococcus xanthus, Rattus norvegicus
Manually annotated by BRENDA team
Fischbach, M.A.; Settleman, J.
Specific biochemical inactivation of oncogenic Ras proteins by nucleoside diphosphate kinase
Cancer Res.
63
4089-4094
2003
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Giraud, M.F.; Georgescauld, F.; Lascu, I.; Dautant, A.
Crystal structures of S120G mutant and wild type of human nucleoside diphosphate kinase A in complex with ADP
J. Bioenerg. Biomembr.
38
261-264
2006
Homo sapiens
Manually annotated by BRENDA team
Mocan, I.; Georgescauld, F.; Gonin, P.; Thoraval, D.; Cervoni, L.; Giartosio, A.; Dabernat-Arnaud, S.; Crouzet, M.; Lacombe, M.; Lascu, I.
Protein phosphorylation corrects the folding defect of the neuroblastoma (S120G) mutant of human nucleoside diphosphate kinase A/Nm23-H1
Biochem. J.
403
149-156
2007
Homo sapiens (P15531), Homo sapiens
Manually annotated by BRENDA team
Morin-Leisk, J.; Lee, T.H.
Nucleotide-dependent self-assembly of nucleoside diphosphate kinase (NDPK) in vitro
Biochim. Biophys. Acta
1784
2045-2051
2008
Homo sapiens
Manually annotated by BRENDA team
Rumjahn, S.M.; Javed, M.A.; Wong, N.; Law, W.E.; Buxton, I.L.
Purinergic regulation of angiogenesis by human breast carcinoma-secreted nucleoside diphosphate kinase
Br. J. Cancer
97
1372-1380
2007
Homo sapiens
Manually annotated by BRENDA team
Tokarska-Schlattner, M.; Boissan, M.; Munier, A.; Borot, C.; Mailleau, C.; Speer, O.; Schlattner, U.; Lacombe, M.L.
The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration
J. Biol. Chem.
283
26198-26207
2008
Rattus norvegicus, Homo sapiens (O00746), Homo sapiens
Manually annotated by BRENDA team
Wieland, T.
Interaction of nucleoside diphosphate kinase B with heterotrimeric G protein betagamma dimers: consequences on G protein activation and stability
Naunyn Schmiedebergs Arch. Pharmacol.
374
373-383
2007
Rattus norvegicus, Homo sapiens (P15531)
Manually annotated by BRENDA team
Schlattner, U.; Tokarska-Schlattner, M.; Ramirez, S.; Brueckner, A.; Kay, L.; Polge, C.; Epand, R.F.; Lee, R.M.; Lacombe, M.L.; Epand, R.M.
Mitochondrial kinases and their molecular interaction with cardiolipin
Biochim. Biophys. Acta
1788
2032-2047
2009
Homo sapiens (O00746)
Manually annotated by BRENDA team
Treharne, K.J.; Best, O.G.; Mehta, A.
The phosphorylation status of membrane-bound nucleoside diphosphate kinase in epithelia and the role of AMP
Mol. Cell. Biochem.
329
107-114
2009
Ovis aries, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Francois-Moutal, L.; Maniti, O.; Marcillat, O.; Granjon, T.
New insights into lipid-nucleoside diphosphate kinase-D interaction mechanism: protein structural changes and membrane reorganisation
Biochim. Biophys. Acta
1828
906-915
2013
Homo sapiens
Manually annotated by BRENDA team
Conery, A.R.; Sever, S.; Harlow, E.
Nucleoside diphosphate kinase Nm23-H1 regulates chromosomal stability by activating the GTPase dynamin during cytokinesis
Proc. Natl. Acad. Sci. USA
107
15461-15466
2010
Homo sapiens
Manually annotated by BRENDA team
Borthwick, L.A.; Kerbiriou, M.; Taylor, C.J.; Cozza, G.; Lascu, I.; Postel, E.H.; Cassidy, D.; Trouve, P.; Mehta, A.; Robson, L.; Muimo, R.
Role of interaction and nucleoside diphosphate kinase B in regulation of the cystic fibrosis transmembrane conductance regulator function by cAMP-dependent protein kinase A
PLoS ONE
11
e0149097
2016
Homo sapiens (P22392)
Manually annotated by BRENDA team
Adam, K.; Lesperance, J.; Hunter, T.; Zage, P.
The potential functional roles of NME1 histidine kinase activity in neuroblastoma pathogenesis
Int. J. Mol. Sci.
21
3319
2020
Homo sapiens (P15531)
Manually annotated by BRENDA team
Hoff, S.; Epting, D.; Falk, N.; Schroda, S.; Braun, D.A.; Halbritter, J.; Hildebrandt, F.; Kramer-Zucker, A.; Bergmann, C.; Walz, G.; Lienkamp, S.S.
The nucleoside-diphosphate kinase NME3 associates with nephronophthisis proteins and is required for ciliary function during renal development
J. Biol. Chem.
293
15243-15255
2018
Xenopus laevis, Homo sapiens (Q13232), Homo sapiens, Danio rerio (Q9PTF3), Danio rerio
Manually annotated by BRENDA team
Lacombe, M.L.; Tokarska-Schlattner, M.; Boissan, M.; Schlattner, U.
The mitochondrial nucleoside diphosphate kinase (NDPK-D/NME4), a moonlighting protein for cell homeostasis
Lab. Invest.
98
582-588
2018
Xenopus laevis, Homo sapiens (O00746), Mus musculus (Q9WV84)
Manually annotated by BRENDA team