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Information on EC 2.7.4.6 - nucleoside-diphosphate kinase and Organism(s) Escherichia coli and UniProt Accession P0A763

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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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This record set is specific for:
Escherichia coli
UNIPROT: P0A763
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The taxonomic range for the selected organisms is: Escherichia coli
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)
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NDK
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nucleoside 5'-diphosphate kinase
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nucleoside diphosphate (UDP) kinase
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nucleoside diphosphate kinase
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nucleoside diphosphokinase
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nucleotide phosphate kinase
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UDP kinase
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uridine diphosphate kinase
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additional information
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enzyme is able to specifically interact with proteins encoded by the bacteriophage T4
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + NDP
ADP + NTP
show the reaction diagram
GTP-bound Ras protein + NDP
GDP-bound Ras protein + NTP
show the reaction diagram
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in vitro, inactivation of mutant oncogenic Ras proteins
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?
NDP + NTP
NTP + NDP
show the reaction diagram
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overview: functions in the cell
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r
NTP + nucleoside diphosphate
NDP + NTP
show the reaction diagram
additional information
?
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NDPK catalyzes the transfer of gamma-phosphate from nucleoside triphosphates to nucleoside diphosphates
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?
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 + NDP
ADP + NTP
show the reaction diagram
NDP + NTP
NTP + NDP
show the reaction diagram
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overview: functions in the cell
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r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Desdanine
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irreversible, specific inhibitor, kinetics, ATP protects, not dTDP or bovine serum albumin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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specific activities of a variety of animals, plants and microorganisms
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
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x * 15000, SDS-PAGE
16000
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x * 16000, deduced from gene sequence
16500
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x * 16500, SDS-PAGE
55000
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gel filtration
additional information
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comparison of kinase amino acid sequences
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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the enzyme shows a tetrameric quaternary structure, the relative orientation of interacting dimers facing either the convex or the concave side of their central sheet, overview
additional information
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recombinant nucleoside-diphosphate kinase interacts with uracil DNA-glycosylase Ung in specific and direct manner. The interaction significantly augments Ung catalytic activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in the enzyme tetramer, subunits interact by an interface harboring the Kpn loop as in hexamers, but at the opposite side of this loop
purified recombinant enzyme, sitting drop vapor diffusion method, mixing 200 nL of protein solution, containing 15 mg/mL protein, with 200 nL of reservoir solution containing 0.2 M ammonium sulphate, 0.1 M sodium acetate/acetic acid buffer, pH 4.6, with either 30% PEG 2000 monomethyl ether or 25% PEG 4000, 20°C, a few hours, X-ray diffraction structure determination and analysis at 1.62 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from strain BL21(DE3) by anion exchange chromatography, ammonium sulfate fractionation, dialysis, and gel filtration
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recombinant protein
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recombinant proteins
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Tuner(DE3)pLysS
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expressed with and without His-tag in Escherichia coli
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gene ndk, overexpressionin strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Allen, J.R.; Lasser, G.W.; Goldman, D.A.; Booth, J.W.; Mathews, C.K.
T4 phage deoxyribonucleotide-synthesizing enzyme complex. Further studies on enzyme composition and regulation
J. Biol. Chem.
258
5746-5753
1983
Escherichia coli
Manually annotated by BRENDA team
Saeki, T.; Hori, M.; Umezawa, H.
Kinetic studies on the inhibition of nucleoside diphosphate kinase by desdanine
J. Biochem.
76
623-629
1974
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Hama, H.; Almaula, N.; Lerner, C.G.; Inouye, S.; Inoue, M.
Nucleoside diphosphate kinase from Escherichia coli; its overproduction and sequence comparison with eukaryotic enzymes
Gene
105
31-36
1991
Escherichia coli
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
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Manually annotated by BRENDA team
Shen, R.; Olcott, M.C.; Kim, J.; Rajagopal, I.; Mathews, C.K.
Escherichia coli nucleoside diphosphate kinase interactions with T4 phage proteins of deoxyribonucleotide synthesis and possible regulatory functions
J. Biol. Chem.
279
32225-32232
2004
Escherichia coli
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
Kumar, P.; Krishna, K.; Srinivasan, R.; Ajitkumar, P.; Varshney, U.
Mycobacterium tuberculosis and Escherichia coli nucleoside diphosphate kinases lack multifunctional activities to process uracil containing DNA
DNA Repair
3
1483-1492
2004
Escherichia coli, Mycobacterium tuberculosis
Manually annotated by BRENDA team
Goswami, S.C.; Yoon, J.H.; Abramczyk, B.M.; Pfeifer, G.P.; Postel, E.H.
Molecular and functional interactions between Escherichia coli nucleoside-diphosphate kinase and the uracil-DNA glycosylase Ung
J. Biol. Chem.
281
32131-32139
2006
Escherichia coli
Manually annotated by BRENDA team
Moynie, L.; Giraud, M.; Georgescauld, F.; Lascu, I.; Dautant, A.
The structure of the Escherichia coli nucleoside diphosphate kinase reveals a new quaternary architecture for this enzyme family
Proteins Struct. Funct. Bioinform.
67
755-765
2007
Escherichia coli (P0A763), Escherichia coli
Manually annotated by BRENDA team
Moynie, L.; Giraud, M.; Georgescauld, F.; Lascu, I.; Dautant, A.
The structure of the Escherichia coli nucleoside diphosphate kinase reveals a new quaternary architecture for this enzyme family
Proteins
67
755-765
2007
Escherichia coli
Manually annotated by BRENDA team