Ethanolamine ammonia-lyase

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In enzymology, an ethanolamine ammonia-lyase (EC 4.3.1.7) is an enzyme that catalyzes the chemical reaction

ethanolamine $\rightleftharpoons$ acetaldehyde + NH₃

Hence, this enzyme has one substrate, ethanolamine, and two products, acetaldehyde and 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). This enzyme is also called ethanolamine deaminase. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, cobamide.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QEZ.

[edit] References

IUBMB entry for 4.3.1.7
BRENDA references for 4.3.1.7 (Recommended.)
PubMed references for 4.3.1.7
PubMed Central references for 4.3.1.7
Google Scholar references for 4.3.1.7
Bradbeer C (1965). "The clostridial fermentations of choline and ethanolamine. 1 Preparation and properties of cell-free extracts". J. Biol. Chem. 240: 4669–74. 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: 4675–81. 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: 1787–93. PMID 4297225.