Nucleotide diphosphokinase

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In enzymology, a nucleotide diphosphokinase (EC 2.7.6.4) is an enzyme that catalyzes the chemical reaction

ATP + nucleoside 5'-phosphate $\rightleftharpoons$ AMP + 5'-phosphonucleoside 3'-diphosphate

Thus, the two substrates of this enzyme are ATP and nucleoside 5'-phosphate, whereas its two products are AMP and 5'-phosphonucleoside 3'-diphosphate.

This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:nucleoside-5'-phosphate diphosphotransferase. Other names in common use include nucleotide pyrophosphokinase, ATP:nucleotide pyrophosphotransferase, ATP nucleotide 3'-pyrophosphokinase, and nucleotide 3'-pyrophosphokinase.

[edit] References

IUBMB entry for 2.7.6.4
BRENDA references for 2.7.6.4 (Recommended.)
PubMed references for 2.7.6.4
PubMed Central references for 2.7.6.4
Google Scholar references for 2.7.6.4
Murao S and Nishino T (1974). "Isolation and identification of ATP:nucleotide pyrophosphotransferase-producing microorganism". Agric. Biol. Chem. 38: 2483–2489.
Nishino T and Murao S (1974). "Purification and some properties of ATP:nucleotide pyrophosphotransferase of Streptomyces adephospholyticus". Agric. Biol. Chem. 38: 2491–2496.
Nishino T and Murao S (1975). "Characterization of pyrophosphoryl transfer reaction of ATP:nucleotide pyrophosphotransferase". Agric. Biol. Chem. 39: 1007–1014.