Lyase

<p>In <a href="/facts/Biochemistry/fa2pWEBp">biochemistry</a>, a lyase is an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> that catalyzes the <a href="/facts/Bond_cleavage/0qtsla4l">breaking</a> (an <a href="/facts/Elimination_reaction/7LSBwU3P">elimination reaction</a>) of various <a href="/facts/Chemical_bond/ArNUMnIB">chemical bonds</a> by means other than <a href="/facts/Hydrolysis/JTvwIHPs">hydrolysis</a> (a <a href="/facts/Substitution_reaction/zpqsbWAo">substitution reaction</a>) and <a href="/facts/Oxidation/Pyd5RVcj">oxidation</a>, often forming a new <a href="/facts/Double_bond/qDemMn0c">double bond</a> or a new <a href="/facts/Ring_(chemistry)/EVFmy88Q">ring structure</a>. The reverse reaction is also possible (called a <a href="/facts/Michael_reaction/yqLD22AQ">Michael reaction</a>). For example, an enzyme that catalyzed this reaction would be a lyase:
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<a href="/facts/Adenosine_triphosphate/nB9bwgcU">ATP</a> → <a href="/facts/Cyclic_adenosine_monophosphate/flK2vwUe">cAMP</a> + PPi
<p>Lyases differ from other enzymes in that they require only one <a href="/facts/Substrate_(chemistry)/6MnaV19h">substrate</a> for the reaction in one direction, but two substrates for the reverse reaction.
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Lyase open-in-new

Lyase