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| | <StructureSection load='4yws' size='340' side='right'caption='[[4yws]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='4yws' size='340' side='right'caption='[[4yws]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yws]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlaa Chlaa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YWS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yws]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexus_aurantiacus_J-10-fl Chloroflexus aurantiacus J-10-fl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YWS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z17|4z17]], [[4z1y|4z1y]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </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=4yws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yws OCA], [https://pdbe.org/4yws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yws RCSB], [https://www.ebi.ac.uk/pdbsum/4yws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yws ProSAT]</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=4yws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yws OCA], [http://pdbe.org/4yws PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yws RCSB], [http://www.ebi.ac.uk/pdbsum/4yws PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yws ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ENO_CHLAA ENO_CHLAA]] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | + | [https://www.uniprot.org/uniprot/ENO_CHLAA ENO_CHLAA] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Enolase|Enolase]] | + | *[[Enolase 3D structures|Enolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlaa]] | + | [[Category: Chloroflexus aurantiacus J-10-fl]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphopyruvate hydratase]]
| + | [[Category: Peters JW]] |
| - | [[Category: Peters, J W]] | + | [[Category: Zadvornyy OA]] |
| - | [[Category: Zadvornyy, O A]] | + | |
| - | [[Category: Enolase]]
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| - | [[Category: Lyase]]
| + | |
| - | [[Category: Phylogeny]]
| + | |
| - | [[Category: Thermophilic origin]]
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| - | [[Category: Thermostability]]
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| Structural highlights
Function
ENO_CHLAA Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Publication Abstract from PubMed
Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis, and is required by all three domains of life. Here, we report the purification and biochemical and structural characterization of enolase from Chloroflexus aurantiacus, a thermophilic anoxygenic phototroph affiliated with the green non-sulfur bacteria. The protein was purified as a homodimer with a subunit molecular weight of 46 kDa. The temperature optimum for enolase catalysis was 80 degrees C, close to the measured thermal stability of the protein which was determined to be 75 degrees C, while the pH optimum for enzyme activity was 6.5. The specific activities of purified enolase determined at 25 and 80 degrees C were 147 and 300 U mg(-1) of protein, respectively. K m values for the 2-phosphoglycerate/phosphoenolpyruvate reaction determined at 25 and 80 degrees C were 0.16 and 0.03 mM, respectively. The K m values for Mg(2+) binding at these temperatures were 2.5 and 1.9 mM, respectively. When compared to enolase from mesophiles, the biochemical and structural properties of enolase from C. aurantiacus are consistent with this being thermally adapted. These data are consistent with the results of our phylogenetic analysis of enolase, which reveal that enolase has a thermophilic origin.
Biochemical and Structural Characterization of Enolase from Chloroflexus aurantiacus: Evidence for a Thermophilic Origin.,Zadvornyy OA, Boyd ES, Posewitz MC, Zorin NA, Peters JW Front Bioeng Biotechnol. 2015 Jun 1;3:74. doi: 10.3389/fbioe.2015.00074., eCollection 2015. PMID:26082925[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zadvornyy OA, Boyd ES, Posewitz MC, Zorin NA, Peters JW. Biochemical and Structural Characterization of Enolase from Chloroflexus aurantiacus: Evidence for a Thermophilic Origin. Front Bioeng Biotechnol. 2015 Jun 1;3:74. doi: 10.3389/fbioe.2015.00074., eCollection 2015. PMID:26082925 doi:http://dx.doi.org/10.3389/fbioe.2015.00074
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