Ethanolamine kinase

Ethanolamine kinase
Identifiers
EC no.2.7.1.82
CAS no.9075-78-9
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

Ethanolamine kinase (EC 2.7.1.82) is an enzyme that catalyzes the chemical reaction

ATP +
 
 
 
 
Reversible left-right reaction arrow
 
 
 
ADP +
 

The enzyme first characterised from Ehrlich ascites cells converts ethanolamine to phosphorylethanolamine by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2][3]

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:ethanolamine O-phosphotransferase. Other names in common use include ethanolamine kinase (phosphorylating), and ethanolamine phosphokinase.[4]

References

  1. ↑ Sung CP, Johnstone RM (1967). "Phosphorylation of choline and ethanolamine in Ehrlich ascites-carcinoma cells". Biochem. J. 105 (2): 497–503. doi:10.1042/bj1050497. PMC 1198337. PMID 5626092.
  2. ↑ 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.
  3. ↑ 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. doi:10.1042/bst0020133.
  4. ↑ Enzyme 2.7.1.82 at KEGG Pathway Database.