Ethanolamine-phosphate phospho-lyase
| ethanolamine-phosphate phospho-lyase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.2.3.2 | ||||||||
| CAS number | 37290-88-3 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, an ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) is an enzyme that catalyzes the chemical reaction
- ethanolamine phosphate + H2O
acetaldehyde + NH3 + phosphate
Thus, the two substrates of this enzyme are ethanolamine phosphate and H2O, whereas its 3 products are acetaldehyde, NH3, and phosphate.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is ethanolamine-phosphate phosphate-lyase (deaminating acetaldehyde-forming). Other names in common use include O-phosphoethanolamine-phospholyase, amino alcohol O-phosphate phospholyase, O-phosphorylethanol-amine phospho-lyase, and ethanolamine-phosphate phospho-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
References
- Fleshood HL, Pitot HC (1970). "The metabolism of O-phosphorylethanolamine in animal tissues. I O-phosphorylethanolamine phospho-lyase: partial purification and characterization". J. Biol. Chem. 245 (17): 4414–20. PMID 5498429.
- Jones A, Faulkner A, Turner JM (1973). "Microbial metabolism of amino alcohols. Metabolism of ethanolamine and 1-aminopropan-2-ol in species of Erwinia and the roles of amino alcohol kinase and amino alcohol o-phosphate phospho-lyase in aldehyde formation". Biochem. J. 134 (4): 959–68. PMC 1177904. PMID 4357716.
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