Deoxyadenosine kinase
| Deoxyadenosine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.76 | ||||||||
| CAS no. | 37278-12-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Deoxyadenosine kinase (EC 2.7.1.76) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from calf thymus and from L1210 cells converts deoxyadenosine to deoxyadenosine monophosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2]
This enzyme is a transferase, specifically one 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.[3]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 2JAQ.
References
- ↑ 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.
- ↑ 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.
- ↑ Enzyme 2.7.1.76 at KEGG Pathway Database.
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