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| | ==Crystal structure of native 4-OT from Pseudomonas putida mt-2 at 1.94 Angstrom== | | ==Crystal structure of native 4-OT from Pseudomonas putida mt-2 at 1.94 Angstrom== |
| - | <StructureSection load='4x19' size='340' side='right' caption='[[4x19]], [[Resolution|resolution]] 1.94Å' scene=''> | + | <StructureSection load='4x19' size='340' side='right'caption='[[4x19]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4x19]] is a 30 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X19 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4x19]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X19 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.944Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></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=4x19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x19 OCA], [http://pdbe.org/4x19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x19 RCSB], [http://www.ebi.ac.uk/pdbsum/4x19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x19 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4x19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x19 OCA], [https://pdbe.org/4x19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x19 RCSB], [https://www.ebi.ac.uk/pdbsum/4x19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x19 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2-hydroxymuconate tautomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Poddar, H]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: Thunnissen, A M.W H]] | + | [[Category: Poddar H]] |
| - | [[Category: 4-oxalocrotonate tautomerase]] | + | [[Category: Thunnissen AMWH]] |
| - | [[Category: Beta-alpha-beta structural motif]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Tautomerase superfamily]]
| + | |
| Structural highlights
Function
4OT1_PSEPU Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP. 4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer. J Biol Chem. 1992 Sep 5;267(25):17716-21. PMID:1339435
- ↑ Poddar H, Rahimi M, Geertsema EM, Thunnissen AM, Poelarends GJ. Evidence for the Formation of an Enamine Species during Aldol and Michael-type Addition Reactions Promiscuously Catalyzed by 4-Oxalocrotonate Tautomerase. Chembiochem. 2015 Feb 26. doi: 10.1002/cbic.201402687. PMID:25728471 doi:http://dx.doi.org/10.1002/cbic.201402687
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