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4wlj

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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=4wlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wlj RCSB], [http://www.ebi.ac.uk/pdbsum/4wlj 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=4wlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wlj RCSB], [http://www.ebi.ac.uk/pdbsum/4wlj PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes 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.<ref>PMID:19338303</ref>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 17:05, 25 December 2014

High resolution crystal structure of human kynurenine aminotransferase-I in complex with aminooxyacetate

4wlj, resolution 1.54Å

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