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| | <StructureSection load='2vun' size='340' side='right'caption='[[2vun]], [[Resolution|resolution]] 1.89Å' scene=''> | | <StructureSection load='2vun' size='340' side='right'caption='[[2vun]], [[Resolution|resolution]] 1.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"inflabilis_barati"_(sic)_prevot_1938 "inflabilis barati" (sic) prevot 1938]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VUN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vun]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"inflabilis_barati"_(sic)_prevot_1938 "inflabilis barati" (sic) prevot 1938]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VUN FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enamidase Enamidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.18 3.5.2.18] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Enamidase Enamidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.18 3.5.2.18] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vun OCA], [http://pdbe.org/2vun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vun RCSB], [http://www.ebi.ac.uk/pdbsum/2vun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vun 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=2vun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vun OCA], [https://pdbe.org/2vun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vun RCSB], [https://www.ebi.ac.uk/pdbsum/2vun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vun ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ENA_EUBBA ENA_EUBBA]] Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.<ref>PMID:16894175</ref> <ref>PMID:18805424</ref> | + | [[https://www.uniprot.org/uniprot/ENA_EUBBA ENA_EUBBA]] Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.<ref>PMID:16894175</ref> <ref>PMID:18805424</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[ENA_EUBBA] Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The hydrolysis of 1,4,5,6-tetrahydro-6-oxonicotinate to 2-formylglutarate is a central step in the catabolism of nicotinate in several Clostridia and Proteobacteria. This reaction is catalyzed by the novel enzyme enamidase, a new member of the amidohydrolase superfamily as indicated by its unique reaction, sequence relationship, and the stoichiometric binding of iron and zinc. A hallmark of enamidase is its capability to catalyze a two-step reaction: the initial decyclization of 1,4,5,6-tetrahydro-6-oxonicotinate leading to 2-(enamine)glutarate followed by an additional hydrolysis step yielding (S)-2-formylglutarate. Here, we present the crystal structure of enamidase from Eubacterium barkeri at 1.9 A resolution, providing a structural basis for catalysis and suggesting a mechanism for its exceptional activity and enantioselectivity. The enzyme forms a 222-symmetric tetramer built up by a dimer of dimers. Each enamidase monomer consists of a composite beta-sandwich domain and an (alpha/beta)(8)-TIM-barrel domain harboring the active site. With its catalytic binuclear metal center comprising both zinc and iron ions, enamidase represents a special case of subtype II amidohydrolases.
The crystal structure of enamidase: a bifunctional enzyme of the nicotinate catabolism.,Kress D, Alhapel A, Pierik AJ, Essen LO J Mol Biol. 2008 Dec 26;384(4):837-47. Epub 2008 Sep 12. PMID:18805424[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12341-6. Epub 2006 Aug 7. PMID:16894175 doi:http://dx.doi.org/10.1073/pnas.0601635103
- ↑ Kress D, Alhapel A, Pierik AJ, Essen LO. The crystal structure of enamidase: a bifunctional enzyme of the nicotinate catabolism. J Mol Biol. 2008 Dec 26;384(4):837-47. Epub 2008 Sep 12. PMID:18805424 doi:http://dx.doi.org/S0022-2836(08)01115-7
- ↑ Kress D, Alhapel A, Pierik AJ, Essen LO. The crystal structure of enamidase: a bifunctional enzyme of the nicotinate catabolism. J Mol Biol. 2008 Dec 26;384(4):837-47. Epub 2008 Sep 12. PMID:18805424 doi:http://dx.doi.org/S0022-2836(08)01115-7
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