4fdx: Difference between revisions
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==Kinetic and structural characterization of the 4-oxalocrotonate tautomerase isozymes from Methylibium petroleiphilum== | ==Kinetic and structural characterization of the 4-oxalocrotonate tautomerase isozymes from Methylibium petroleiphilum== | ||
<StructureSection load='4fdx' size='340' side='right' caption='[[4fdx]], [[Resolution|resolution]] 1.64Å' scene=''> | <StructureSection load='4fdx' size='340' side='right' caption='[[4fdx]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mpe_A3323 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=420662 METPP])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mpe_A3323 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=420662 METPP])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxaloacetate_tautomerase Oxaloacetate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.2 5.3.2.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxaloacetate_tautomerase Oxaloacetate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.2 5.3.2.2] </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=4fdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fdx RCSB], [http://www.ebi.ac.uk/pdbsum/4fdx 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=4fdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdx OCA], [http://pdbe.org/4fdx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fdx RCSB], [http://www.ebi.ac.uk/pdbsum/4fdx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4fdx" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 16:45, 11 August 2016
Kinetic and structural characterization of the 4-oxalocrotonate tautomerase isozymes from Methylibium petroleiphilumKinetic and structural characterization of the 4-oxalocrotonate tautomerase isozymes from Methylibium petroleiphilum
Structural highlights
Publication Abstract from PubMedMethylibium petroleiphilum strain PM1 uses various petroleum products including the fuel additive methyl tert-butyl ether and straight chain and aromatic hydrocarbons as sole carbon and energy sources. It has two operons, dmpI and dmpII, that code for the enzymes in a pair of parallel meta-fission pathways. In order to understand the roles of the pathways, the 4-oxalocrotonate tautomerase (4-OT) isozyme from each pathway was characterized. Tautomerase I and tautomerase II have the lowest pairwise sequence identity (35%) among the isozyme pairs in the parallel pathways, and could offer insight into substrate preferences and pathway functions. The kinetic parameters of tautomerase I and tautomerase II were determined using 2-hydroxymuconate and 5-(methyl)-2-hydroxymuconate. Both tautomerase I and tautomerase II process the substrates, but with different efficiencies. Crystal structures were determined for both tautomerase I and tautomerase II, at 1.57 and 1.64A resolution, respectively. The backbones of tautomerase I and tautomerase II are highly similar, but have distinct active site environments. The results, in combination with those for other structurally and kinetically characterized 4-OT isozymes, suggest that tautomerase I catalyzes the tautomerization of both 2-hydroxymuconate and alkyl derivatives, whereas tautomerase II might specialize in other aromatic hydrocarbon metabolites. Structural and kinetic characterization of two 4-oxalocrotonate tautomerases in Methylibium petroleiphilum strain PM1.,Terrell CR, Burks EA, Whitman CP, Hoffman DW Arch Biochem Biophys. 2013 Sep 1;537(1):113-24. doi: 10.1016/j.abb.2013.06.016., Epub 2013 Jul 4. PMID:23831510[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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