Ethanolamine_kinase

Ethanolamine kinase

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 ADP + O-phosphoethanolamine
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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

    • 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.


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