| EC |
4.2.3.2 |
| Accepted name: |
ethanolamine-phosphate phospho-lyase |
| Reaction: |
ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate |
| Other name(s): |
O-phosphoethanolamine-phospholyase; amino alcohol O-phosphate phospholyase; O-phosphorylethanol-amine phospho-lyase; ethanolamine-phosphate phospho-lyase (deaminating) |
| Systematic name: |
ethanolamine-phosphate phosphate-lyase (deaminating; acetaldehyde-forming) |
| Comments: |
A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37290-88-3 |
| References: |
| 1. |
Fleshood, H.L. and Pitot, H.C. The metabolism of O-phosphorylethanolamine in animal tissues. I. O-Phosphorylethanolamine phospho-lyase: partial purification and characterization. J. Biol. Chem. 245 (1970) 4414–4420. [PMID: 5498429] |
| 2. |
Jones, A., Faulkner, A. and Turner, J.M. 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 (1973) 959–968. [PMID: 4357716] |
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| [EC 4.2.3.2 created 1972 as EC 4.2.99.7, transferred 2000 to EC 4.2.3.2] |
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