Adenosine kinase

From Wikipedia, the free encyclopedia

In enzymology, an adenosine kinase (EC 2.7.1.20) is an enzyme that catalyzes the chemical reaction

ATP + adenosine $\rightleftharpoons$ ADP + AMP

Thus, the two substrates of this enzyme are ATP and adenosine, whereas its two products are ADP and AMP.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:adenosine 5'-phosphotransferase. This enzyme is also called adenosine kinase (phosphorylating). This enzyme participates in purine metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 1BX4, 1DGM, 1LII, 1LIJ, 1LIK, 1LIO, 2A9Y, 2A9Z, 2AA0, 2AB8, 2ABS, 2GL0, 2PKF, 2PKK, 2PKM, and 2PKN.

[edit] References

IUBMB entry for 2.7.1.20
BRENDA references for 2.7.1.20 (Recommended.)
PubMed references for 2.7.1.20
PubMed Central references for 2.7.1.20
Google Scholar references for 2.7.1.20
Lindberg B, Klenow H, Hansen K (1967). "Some properties of partially purified mammalian adenosine kinase". J. Biol. Chem. 242: 350–6. PMID 4290214.
CAPUTTO R (1951). "The enzymatic synthesis of adenylic acid; adenosinekinase". J. Biol. Chem. 189: 801–14. PMID 14832298.
Kornberg A and Pricer WE (1951). "Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside". J. Biol. Chem. 193: 481–495.