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

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

Stable Identifier

R-HSA-482619

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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

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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		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