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4.2.3.2 |
Description |
Ethanolamine-phosphate phospho-lyase |
Catalyzed reaction |
Ethanolamine phosphate + H(2)O = acetaldehyde + NH(3) + phosphate. |
Cofactor |
Pyridoxal-phosphate. |
Comments |
-!- Also acts on D- (or L)-1-aminopropan-2-ol O-phosphate. -!- Formerly EC 4.2.99.7. |
PDB |
5G4J; |
Organisms |
-Eubacteria -Metazoa -Human |
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Family |
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Links |
Enzyme (activities) 4.2.3.2
BRENDA (activities) 4.2.3.2
KEGG (pathways) 4.2.3.2
PLPMDB (PLP mutants) 4.2.3.2
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References |
Cuetos A, Steffen-Munsberg F, Mangas Sanchez J, Frese A, Bornscheuer UT, Höhne M, Grogan G (2016) Structural Basis for Phospholyase Activity of a Class III Transaminase Homologue Chembiochem 17 2308-2311. Schiroli, D.; Cirrincione, S.; Donini, S.; Peracchi, A. (2013) Strict reaction and substrate specificity of AGXT2L1, the human O-phosphoethanolamine phospho-lyase IUBMB Life 65 645-50. Veiga-da-Cunha, M., Hadi, F., Balligand, T., Stroobant, V. and Van Schaftingen, E. (2012) Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine. J. Biol. Chem. 287 7246-7255. Fleshood, H. L.; Pitot, H. C. (1970) The metabolism of O-phosphorylethanolamine in animal tissues. I. O- phosphorylethanolamine phospho-lyase: partial purification and characterization J Biol Chem 245 4414-20. Articles on 4.2.3.2 |
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last changed |
2019/02/13 15:55 |
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