Adenosine kinase
| adenosine kinase | |||||||
|---|---|---|---|---|---|---|---|
| Cartoon representation of the molecular structure of protein registered with 1lio code. | |||||||
| Identifiers | |||||||
| EC number | 2.7.1.20 | ||||||
| CAS number | 9027-72-9 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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In enzymology, an adenosine kinase (EC 2.7.1.20) is an enzyme that catalyzes the chemical reaction
- ATP + adenosine
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.
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.
References
- Lindberg B, Klenow H, Hansen K (1967). "Some properties of partially purified mammalian adenosine kinase". J. Biol. Chem. 242 (3): 350–6. PMID 4290214.
- CAPUTTO R (1951). "The enzymatic synthesis of adenylic acid; adenosinekinase". J. Biol. Chem. 189 (2): 801–14. PMID 14832298.
- Kornberg A and Pricer WE (1951). "Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside". J. Biol. Chem. 193 (2): 481–495. PMID 14907737.