Ethanolamine ammonia-lyase

The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction

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
Search PMC articles PubMed articles NCBI proteins

ethanolamine $\rightleftharpoons$ 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

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

• 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.