Ethanolamine kinase

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In enzymology, an ethanolamine kinase (EC 2.7.1.82) is an enzyme that catalyzes the chemical reaction

ATP + ethanolamine $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 2.7.1.82
BRENDA references for 2.7.1.82 (Recommended.)
PubMed references for 2.7.1.82
PubMed Central references for 2.7.1.82
Google Scholar references for 2.7.1.82
Faulkner A and 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: 497–503. PMID 5626092.
Weinhold PA, Rethy VB (1972). "Ethanolamine phosphokinase: activity and properties during liver development". Biochim. Biophys. Acta. 276: 143–54. PMID 5047700.