4x1c: Difference between revisions
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''' | ==Crystal structure of 4-OT from Pseudomonas putida mt-2 with an enamine adduct on the N-terminal proline at 1.7 Angstrom resolution== | ||
<StructureSection load='4x1c' size='340' side='right' caption='[[4x1c]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4x1c]] is a 15 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X1C FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=N80:1-ETHENYL-L-PROLINE'>N80</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-hydroxymuconate_tautomerase 2-hydroxymuconate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.6 5.3.2.6] </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=4x1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x1c RCSB], [http://www.ebi.ac.uk/pdbsum/4x1c PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/4OT1_PSEPU 4OT1_PSEPU]] Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.<ref>PMID:1339435</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The enzyme 4-oxalocrotonate tautomerase (4-OT), which has a catalytic N-terminal proline residue (Pro1), can promiscuously catalyze various carbon-carbon bond-forming reactions, including aldol condensation of acetaldehyde with benzaldehyde to yield cinnamaldehyde, and Michael-type addition of acetaldehyde to a wide variety of nitroalkenes to yield valuable gamma-nitroaldehydes. To gain insight into how 4-OT catalyzes these unnatural reactions, we carried out exchange studies in D2 O, and X-ray crystallography studies. The former established that H-D exchange within acetaldehyde is catalyzed by 4-OT and that the Pro1 residue is crucial for this activity. The latter showed that Pro1 of 4-OT had reacted with acetaldehyde to give an enamine species. These results provide evidence of the mechanism of the 4-OT-catalyzed aldol and Michael-type addition reactions in which acetaldehyde is activated for nucleophilic addition by Pro1-dependent formation of an enamine intermediate. | |||
Evidence for the Formation of an Enamine Species during Aldol and Michael-type Addition Reactions Promiscuously Catalyzed by 4-Oxalocrotonate Tautomerase.,Poddar H, Rahimi M, Geertsema EM, Thunnissen AM, Poelarends GJ Chembiochem. 2015 Feb 26. doi: 10.1002/cbic.201402687. PMID:25728471<ref>PMID:25728471</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: 2-hydroxymuconate tautomerase]] | |||
[[Category: Poddar, H]] | [[Category: Poddar, H]] | ||
[[Category: Thunnissen, A M.W H]] | |||
[[Category: Enamine formation]] | |||
[[Category: Isomerase]] | |||
Revision as of 11:45, 11 March 2015
Crystal structure of 4-OT from Pseudomonas putida mt-2 with an enamine adduct on the N-terminal proline at 1.7 Angstrom resolution
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