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In enzymology, an ethanolamine ammonia-lyase () is an enzyme that catalyzes the chemical reaction :ethanolamine 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, 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 . Later, more structures have become available from Escherichia coli that include both EAL subunits bound to various ligands. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Ethanolamine ammonia-lyase」の詳細全文を読む スポンサード リンク
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