(d)NDP + ATP <=> (d)NTP + ADP (NME1,2,3)

Stable Identifier
Reaction [transition]
Homo sapiens
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Cytosolic nucleoside diphosphate kinases catalyze the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ATP to form the corresponding nucleoside 5'-triphosphates and ADP. These kinases are ubiquitously expressed enzymes with broad substrate specificities (Berg and Joklik 1954; Parks and Agarwal 1973). Three human cytosolic nucleoside diphosphate kinase proteins, NME1, 2, and 3, have been characterized biochemically (Gilles et al. 1991; Schaertl et al. 1998; Erent et al. 2001; Chen et al. 2003). All are catalytically active as hexamers: homohexamers of NME1, 2, and 3 have been described, as have heterohexamers containing all possible combinations of NME1 and 2 (Gilles et al. 1991; Erent et al. 2001).

While cytosolic nucleoside diphosphate kinases can efficiently use several nucleotide triphosphates as a phosphate donor, the high concentrations of ATP relative to other nucleoside triphosphates in vivo makes it the likely major phosphate donor in these reactions and only reactions with ATP as the phosphate donor are annotated. All of these phosphorylation reactions are freely reversible in vitro (Parks and Agarwal 1973; Schaertl et al. 1998), but the high ratio of ATP to ADP concentrations in the cytosol should favor the conversion of (d)NDP and ATP to (d)NTP and ADP.

Literature References
PubMed ID Title Journal Year
  The Enzymes, 3rd ed

Boyer, PD

12972261 Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases

Janin, J, Moréra, S, Schneider, B, Deville-Bonne, D, Veron, M, Gallois-Montbrun, S, Chen, Y

J Mol Biol 2003
1851158 Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme

Vonica, A, Lascu, I, Gilles, AM, Presecan, E

J Biol Chem 1991
13211603 Enzymatic phosphorylation of nucleoside diphosphates

Berg, P, Joklik, WK

J Biol Chem 1954
9488696 Substrate specificity of human nucleoside-diphosphate kinase revealed by transient kinetic analysis

Konrad, M, Geeves, MA, Schaertl, S

J Biol Chem 1998
11277919 Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene

Konrad, M, Agou, F, Lacombe, ML, Sarger, C, Raschella, G, Lascu, I, Giartosio, A, Cherfils, J, Tissier, P, Erent, M, Gonin, P

Eur J Biochem 2001
Event Information
Catalyst Activity

nucleoside diphosphate kinase activity of NME1,2 hexamers [cytosol]

Orthologous Events
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