The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7)
catalyzes
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...
the
chemical reaction
:ethanolamine
acetaldehyde + NH
3
This enzyme belongs to the family of
lyase
In biochemistry, a lyase is an enzyme that catalyzes the breaking (an elimination reaction) of various chemical bonds by means other than hydrolysis (a substitution reaction) and oxidation, often forming a new double bond or a new ring structure. ...
s, 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
Glycerophospholipids or phosphoglycerides are glycerol-based phospholipids. They are the main component of biological membranes. Two major classes are known: those for bacteria and eukaryotes and a separate family for archaea.
Structures
T ...
. 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.
References
*
*
*
EC 4.3.1
Cobamide enzymes
Enzymes of known structure
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