In enzymology, a deoxyadenosine kinase (EC 2.7.1.76) is an enzyme that catalyzes the chemical reaction
| deoxyadenosine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.76 | ||||||||
| CAS no. | 37278-12-9 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
- ATP + deoxyadenosine ADP + dAMP
Thus, the two substrates of this enzyme are ATP and deoxyadenosine, whereas its two products are ADP and dAMP.
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:deoxyadenosine 5'-phosphotransferase. This enzyme is also called purine-deoxyribonucleoside kinase. This enzyme participates in purine metabolism.
Structural studies
editAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2JAQ.
References
edit- Chang CH, Brockman RW, Bennett LL (1982). "Purification and some properties of a deoxyribonucleoside kinase from L1210 cells". Cancer Res. 42 (8): 3033–9. PMID 6284353.
- Krygier V, Momparler RL (1968). "The regulatory properties of deoxyadenosine kinase". Biochim. Biophys. Acta. 161 (2): 578–80. doi:10.1016/0005-2787(68)90139-1. PMID 5667299.
