3e2z

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e2z RCSB], [http://www.ebi.ac.uk/pdbsum/3e2z PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e2z RCSB], [http://www.ebi.ac.uk/pdbsum/3e2z PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/KAT3_MOUSE KAT3_MOUSE]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro).<ref>PMID:19029248</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 21:32, 24 December 2014

Crystal structure of mouse kynurenine aminotransferase III in complex with kynurenine

3e2z, resolution 2.81Å

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