Ethanolamine kinase
| ethanolamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.82 | ||||||||
| CAS no. | 9075-78-9 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an ethanolamine kinase (EC 2.7.1.82) is an enzyme that catalyzes the chemical reaction
- ATP + ethanolamine ADP + O-phosphoethanolamine
Thus, the two substrates of this enzyme are ATP and ethanolamine, whereas its two products are ADP and O-phosphoethanolamine.
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:ethanolamine O-phosphotransferase. Other names in common use include ethanolamine kinase (phosphorylating), and ethanolamine phosphokinase. This enzyme participates in glycerophospholipid metabolism.
References
[edit]- Faulkner A, Turner JM (1974). "Phosphorylation of ethanolamine in catabolism: biodegradative adenosine triphosphate-ethanolamine phosphotransferase and related enzymes in bacteria". Biochem. Soc. Trans. 2: 133–136.
- Sung CP, Johnstone RM (1967). "Phosphorylation of choline and ethanolamine in Ehrlich ascites-carcinoma cells". Biochem. J. 105 (2): 497–503. PMC 1198337. PMID 5626092.
- Weinhold PA, Rethy VB (1972). "Ethanolamine phosphokinase: activity and properties during liver development" (PDF). Biochim. Biophys. Acta. 276 (1): 143–54. doi:10.1016/0005-2744(72)90015-0. hdl:2027.42/34067. PMID 5047700.
