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| | <StructureSection load='4rje' size='340' side='right'caption='[[4rje]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='4rje' size='340' side='right'caption='[[4rje]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rje]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"gaffkya_homari"_hitchner_and_snieszko_1947 "gaffkya homari" hitchner and snieszko 1947]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RJE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rje]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerococcus_viridans Aerococcus viridans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RJE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactate_2-monooxygenase Lactate 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.4 1.13.12.4] </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=4rje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rje OCA], [https://pdbe.org/4rje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rje RCSB], [https://www.ebi.ac.uk/pdbsum/4rje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rje 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=4rje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rje OCA], [http://pdbe.org/4rje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rje RCSB], [http://www.ebi.ac.uk/pdbsum/4rje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rje ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LOX_AERVM LOX_AERVM] Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2 (Ref.1, PubMed:27302031, PubMed:25423902, PubMed:2818595, PubMed:8589073, PubMed:26260739). Cannot oxidize D-lactate, glycolate, and D,L-2-hydroxybutanoate (PubMed:2818595). May be involved in the utilization of L-lactate as an energy source for growth (By similarity).[UniProtKB:O33655]<ref>PMID:25423902</ref> <ref>PMID:26260739</ref> <ref>PMID:27302031</ref> <ref>PMID:2818595</ref> <ref>PMID:8589073</ref> [UniProtKB:O33655] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 17: |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4rje" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4rje" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Gaffkya homari hitchner and snieszko 1947]] | + | [[Category: Aerococcus viridans]] |
| - | [[Category: Lactate 2-monooxygenase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nidetzky, B]] | + | [[Category: Nidetzky B]] |
| - | [[Category: Rainer, D]] | + | [[Category: Rainer D]] |
| - | [[Category: Wilson, D K]] | + | [[Category: Wilson DK]] |
| - | [[Category: Beta/alpha barrel]]
| + | |
| - | [[Category: Fmn]]
| + | |
| - | [[Category: Oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
LOX_AERVM Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2 (Ref.1, PubMed:27302031, PubMed:25423902, PubMed:2818595, PubMed:8589073, PubMed:26260739). Cannot oxidize D-lactate, glycolate, and D,L-2-hydroxybutanoate (PubMed:2818595). May be involved in the utilization of L-lactate as an energy source for growth (By similarity).[UniProtKB:O33655][1] [2] [3] [4] [5] [UniProtKB:O33655]
Publication Abstract from PubMed
Aerococcus viridans L-lactate oxidase (avLOX) is a biotechnologically important flavoenzyme that catalyzes conversion of L-lactate and O2 into pyruvate and H2 O2. The enzymatic reaction underlies different biosensor applications of avLOX for blood L-lactate determination. The ability of avLOX to replace O2 with other electron acceptors such as 2,6-dichlorophenol-indophenol (DCIP) provides possiblities for analytical and practical uses. The A95G variant of avLOX was previously shown to exhibit lowered reactivity with O2 as compared to wild-type enzyme, and it was used here for detailed evaluation of effects on the specificity for different electron acceptor substrates. From stopped-flow experiments performed at 20 degrees C and pH 6.5, we determined that A95G variant (fully reduced by L-lactate) was ~3-fold more reactive towards DCIP (1.0 +/- 0.1 x 106 M-1 s-1 ) than O2 while avLOX wild type under the same conditions was 14-fold more reactive towards O2 (1.8 +/- 0.1 x 106 M-1 s-1 ) than DCIP. Substituted 1,4-benzoquinones were up to 5-fold better electron acceptors for reaction with L-lactate-reduced A95G variant than wild type. A 1.65 A crystal structure of oxidized A95G variant bound with pyruvate was determined and reveals that steric volume created by removal of the methyl side chain of Ala95 and a slight additional shift in the main chain at position Gly95 enable accomodation of a new active-site water molecule within hydrogen bond distance to the N5 of the FMN cofactor. The increased steric volume available in the active site allows the A95G variant to exhibit a similar trend with the the related glycolate oxidase in electron acceptor substrate specificities despite the fact that the latter contains an alanine at the analogous position. This article is protected by copyright. All rights reserved.
The Ala -to-Gly substitution in Aerococcus viridans L-lactate oxidase revisited: structural consequences at the catalytic site and effect on reactivity with O and other electron acceptors.,Stoisser T, Rainer D, Leitgeb S, Wilson DK, Nidetzky B FEBS J. 2014 Nov 25. doi: 10.1111/febs.13162. PMID:25423902[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stoisser T, Rainer D, Leitgeb S, Wilson DK, Nidetzky B. The Ala -to-Gly substitution in Aerococcus viridans L-lactate oxidase revisited: structural consequences at the catalytic site and effect on reactivity with O and other electron acceptors. FEBS J. 2014 Nov 25. doi: 10.1111/febs.13162. PMID:25423902 doi:http://dx.doi.org/10.1111/febs.13162
- ↑ Stoisser T, Klimacek M, Wilson DK, Nidetzky B. Speeding up the product release: a second-sphere contribution from Tyr191 to the reactivity of L-lactate oxidase revealed in crystallographic and kinetic studies of site-directed variants. FEBS J. 2015 Aug 11. doi: 10.1111/febs.13409. PMID:26260739 doi:http://dx.doi.org/10.1111/febs.13409
- ↑ Stoisser T, Brunsteiner M, Wilson DK, Nidetzky B. Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr(215) in Aerococcus viridans lactate oxidase. Sci Rep. 2016 Jun 15;6:27892. doi: 10.1038/srep27892. PMID:27302031 doi:http://dx.doi.org/10.1038/srep27892
- ↑ Duncan JD, Wallis JO, Azari MR. Purification and properties of Aerococcus viridans lactate oxidase. Biochem Biophys Res Commun. 1989 Oct 31;164(2):919-26. PMID:2818595 doi:10.1016/0006-291x(89)91546-5
- ↑ Maeda-Yorita K, Aki K, Sagai H, Misaki H, Massey V. L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a common structural theme. Biochimie. 1995;77(7-8):631-42. PMID:8589073 doi:10.1016/0300-9084(96)88178-8
- ↑ Stoisser T, Rainer D, Leitgeb S, Wilson DK, Nidetzky B. The Ala -to-Gly substitution in Aerococcus viridans L-lactate oxidase revisited: structural consequences at the catalytic site and effect on reactivity with O and other electron acceptors. FEBS J. 2014 Nov 25. doi: 10.1111/febs.13162. PMID:25423902 doi:http://dx.doi.org/10.1111/febs.13162
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