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| | <StructureSection load='6rhs' size='340' side='right'caption='[[6rhs]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6rhs' size='340' side='right'caption='[[6rhs]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rhs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pediococcus_acidilactici_dsm_20284 Pediococcus acidilactici dsm 20284]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RHS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rhs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pediococcus_acidilactici_DSM_20284 Pediococcus acidilactici DSM 20284]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RHS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lctO, HMPREF0623_0568 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=862514 Pediococcus acidilactici DSM 20284])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6rhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhs OCA], [http://pdbe.org/6rhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rhs RCSB], [http://www.ebi.ac.uk/pdbsum/6rhs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhs 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=6rhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhs OCA], [https://pdbe.org/6rhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rhs RCSB], [https://www.ebi.ac.uk/pdbsum/6rhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E0NE46_PEDAC E0NE46_PEDAC] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pediococcus acidilactici dsm 20284]] | + | [[Category: Pediococcus acidilactici DSM 20284]] |
| - | [[Category: Ashok, Y]] | + | [[Category: Ashok Y]] |
| - | [[Category: Kilpelainen, P]] | + | [[Category: Kilpelainen P]] |
| - | [[Category: Lehtio, L]] | + | [[Category: Lehtio L]] |
| - | [[Category: Maksimainen, M M]] | + | [[Category: Maksimainen MM]] |
| - | [[Category: Alpha hydroxyacid]]
| + | |
| - | [[Category: Fmn]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
E0NE46_PEDAC
Publication Abstract from PubMed
Lactate oxidases belong to a group of FMN-dependent enzymes and they catalyze a conversion of lactate to pyruvate with a release of hydrogen peroxide. Hydrogen peroxide is also utilized as a read out in biosensors to quantitate lactate levels in biological samples. Aerococcus viridans lactate oxidase is the best characterized lactate oxidase and our knowledge of lactate oxidases relies largely to studies conducted with that particular enzyme. Pediococcus acidilactici lactate oxidase is also commercially available for e.g. lactate measurements, but this enzyme has not been characterized in detail before. Here we report structural characterization of the recombinant enzyme and its co-factor dependent oligomerization. The crystal structures revealed two distinct conformations in the loop closing the active site, consistent with previous biochemical studies implicating the role of loop in catalysis. Despite the structural conservation of active site residues, we were not able to detect either oxidase or monooxygenase activity when L-lactate was used as a substrate. Pediococcus acidilactici lactate oxidase is therefore an example of a misannotation of an FMN-dependent enzyme, which catalyzes likely a so far unknown oxidation reaction.
FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici.,Ashok Y, Maksimainen MM, Kallio T, Kilpelainen P, Lehtio L PLoS One. 2020 Feb 24;15(2):e0223870. doi: 10.1371/journal.pone.0223870., eCollection 2020. PMID:32092083[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ashok Y, Maksimainen MM, Kallio T, Kilpelainen P, Lehtio L. FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici. PLoS One. 2020 Feb 24;15(2):e0223870. doi: 10.1371/journal.pone.0223870., eCollection 2020. PMID:32092083 doi:http://dx.doi.org/10.1371/journal.pone.0223870
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