Opheline kinase
| opheline kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.7 | ||||||||
| CAS no. | 37278-15-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an opheline kinase (EC 2.7.3.7) is an enzyme that catalyzes the chemical reaction
- ATP + guanidinoethyl methyl phosphate ADP + N'-phosphoguanidinoethyl methylphosphate
Thus, the two substrates of this enzyme are ATP and guanidinoethyl methyl phosphate, whereas its two products are ADP and N'-phosphoguanidinoethyl methylphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoethyl-methyl-phosphate phosphotransferase.
References
[edit]- Thoai NV, di Jeso F, Robin Y, der Terrossian E (1966). "Sur la nouvelle acide adenosine 5'-triphosphorique:guanidine phosphotransferase, l'opheline kinase". Biochim. Biophys. Acta. 113: 542–550. doi:10.1016/s0926-6593(66)80012-7.
