6RHS
Crystal structure of Pediococcus acidilactici (Putative)lactate oxidase Refolded WT protein
6RHS の概要
| エントリーDOI | 10.2210/pdb6rhs/pdb |
| 分子名称 | Putative L-lactate oxidase, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | tim barrel, fmn, alpha hydroxyacid., oxidoreductase |
| 由来する生物種 | Pediococcus acidilactici DSM 20284 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 40359.31 |
| 構造登録者 | Ashok, Y.,Maksimainen, M.M.,Kilpelainen, P.,Lehtio, L. (登録日: 2019-04-22, 公開日: 2020-02-12, 最終更新日: 2024-01-24) |
| 主引用文献 | Ashok, Y.,Maksimainen, M.M.,Kallio, T.,Kilpelainen, P.,Lehtio, L. FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici. Plos One, 15:e0223870-e0223870, 2020 Cited by PubMed Abstract: 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. PubMed: 32092083DOI: 10.1371/journal.pone.0223870 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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