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

Stable Identifier
R-HSA-482621
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Cytosolic nucleoside diphosphate kinases catalyze the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ADP to form the corresponding nucleoside 5'-diphosphates and ATP. 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 the high ratio of ATP to ADP concentrations in the cytosol normally favors the conversion of (d)NDP and ATP to (d)NTP and ADP, the reversibility of the reactions and the overlapping substrate specificities of the enzymes suggest that this group of reverse reactions can buffer the intracellular nucleotide pool and regulate the relative concentrations of individual nucleoside di- and tri-phosphates in the pool.

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

Boyer, PD

  1973
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
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Participates
Catalyst Activity

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

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