Ethanolamine ammonia-lyase
| ethanolamine ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.7 | ||||||||
| CAS no. | 9054-69-7 | ||||||||
| 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 / QuickGO | ||||||||
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The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction
- ethanolamine acetaldehyde + NH3
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is ethanolamine ammonia-lyase (acetaldehyde-forming). It is also called ethanolamine deaminase. It participates in glycerophospholipid metabolism. It employs one cofactor, adenosylcobalamin.
Structural studies[edit]
As of early 2011, several structures have been solved for this class of enzymes. The first structure solved was the active site containing EutB subunit of EAL from Listeria monocytogenes with the PDB accession code 2QEZ. Later, more structures have become available from Escherichia coli that include both EAL subunits bound to various ligands.
References[edit]
- Bradbeer C (1965). "The clostridial fermentations of choline and ethanolamine. 1 Preparation and properties of cell-free extracts". J. Biol. Chem. 240 (12): 4669–74. doi:10.1016/S0021-9258(18)97007-9. PMID 5846987.
- Bradbeer C (1965). "The clostridial fermentations of choline and ethanolamine. II Requirement for a cobamide coenzyme by an ethanolamine deaminase". J. Biol. Chem. 240 (12): 4675–81. doi:10.1016/S0021-9258(18)97008-0. PMID 5846988.
- Kaplan BH, Stadtman ER (1968). "Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. I Purification, assay, and properties of the enzyme". J. Biol. Chem. 243 (8): 1787–93. doi:10.1016/S0021-9258(18)93512-X. PMID 4297225.
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