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3vba

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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=3vba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vba OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vba RCSB], [http://www.ebi.ac.uk/pdbsum/3vba 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=3vba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vba OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vba RCSB], [http://www.ebi.ac.uk/pdbsum/3vba PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/LEUD_METJA LEUD_METJA]] Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.<ref>PMID:17449626</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 22:02, 24 December 2014

Crystal structure of methanogen 3-isopropylmalate isomerase small subunit

3vba, resolution 2.00Å

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