L-dopachrome isomerase

In <a href="/facts/Enzymology/DSI1Fh7y">enzymology</a>, a L-dopachrome isomerase (<a href="/facts/Enzyme_Commission_number/Y5GNLRKX">EC</a> <a href="https://www.enzyme-database.org/query.php?ec=5.3.3.12">5.3.3.12</a>) is an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> that <a href="/facts/Catalysis/LPBS7TQC">catalyzes</a> the <a href="/facts/Chemical_reaction/GpqWlKrz">chemical reaction</a>

L-dopachrome 
 
 
 
 ⇌
 
 
 {\displaystyle \rightleftharpoons }
 
 5,6-dihydroxyindole-2-carboxylate
Hence, this enzyme has one <a href="/facts/Substrate_(biochemistry)/6MnaV19h">substrate</a>, <a href="/facts/L-dopachrome/BfRDPVcX">L-dopachrome</a>, and one <a href="/facts/Product_(chemistry)/8uCoDUdv">product</a>, <a href="/facts/5,6-dihydroxyindole-2-carboxylate/urhM5oBu">5,6-dihydroxyindole-2-carboxylate</a>.
This enzyme belongs to the family of <a href="/facts/Isomerase/DtUWnvle">isomerases</a>, specifically those intramolecular <a href="/facts/Oxidoreductase/neW0G5D4">oxidoreductases</a> transposing C=C bonds. The <a href="/facts/List_of_enzymes/w2RP6EwU">systematic name</a> of this enzyme class is L-dopachrome keto-enol isomerase. Other names in common use include dopachrome tautomerase, tyrosinase-related protein 2, TRP-1, TRP2, TRP-2, tyrosinase-related protein-2, dopachrome Delta7,Delta2-isomerase, dopachrome Delta-isomerase, dopachrome conversion factor, dopachrome isomerase, dopachrome oxidoreductase, dopachrome-rearranging enzyme, DCF, DCT, dopachrome keto-enol isomerase, and L-dopachrome-methyl ester tautomerase. This enzyme participates in <a href="/facts/Tyrosine_metabolism/RJhEgE4C">tyrosine metabolism</a> and <a href="/facts/Melanogenesis/z8KowoXP">melanogenesis</a>.

<ul><li>Jara JR, Lozano JA (January 15, 1996). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1216928">"Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome tautomerase"</a>. Biochem. J. 313 (2): 447–53. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1216928">1216928</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8573077">8573077</a>.</li>
<li>Pawelek JM (1990). <a href="https://doi.org/10.1016%2F0006-291X%2890%2991011-G">"Dopachrome conversion factor functions as an isomerase"</a>. Biochem. Biophys. Res. Commun. 166 (3): 1328–33. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0006-291X%2890%2991011-G">10.1016/0006-291X(90)91011-G</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2106316">2106316</a>.</li>
<li>Joshua GW, Selkirk ME, Zhang Y, Meyer DJ (November 1, 1998). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1219807">"Rapid purification and characterization of L-dopachrome-methyl ester tautomerase (macrophage-migration-inhibitory factor) from Trichinella spiralis, Trichuris muris and Brugia pahangi"</a>. Biochem. J. 335 (3): 495–8. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1219807">1219807</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9794786">9794786</a>.</li></ul>

L-dopachrome isomerase open-in-new

L-dopachrome isomerase