7F20
L-lactate oxidase with L-lactate
Summary for 7F20
| Entry DOI | 10.2210/pdb7f20/pdb |
| Descriptor | L-lactate oxidase, FLAVIN MONONUCLEOTIDE, (2S)-2-HYDROXYPROPANOIC ACID, ... (4 entities in total) |
| Functional Keywords | l-lactate, complex, oxidoreductase |
| Biological source | Aerococcus viridans |
| Total number of polymer chains | 2 |
| Total formula weight | 158679.42 |
| Authors | Morimoto, Y.,Inaka, K. (deposition date: 2021-06-10, release date: 2022-03-23, Last modification date: 2023-11-29) |
| Primary citation | Furubayashi, N.,Inaka, K.,Kamo, M.,Umena, Y.,Matsuoka, T.,Morimoto, Y. Dynamic interactions in the l-lactate oxidase active site facilitate substrate binding at pH4.5. Biochem.Biophys.Res.Commun., 568:131-135, 2021 Cited by PubMed Abstract: The crystal structure of l-lactate oxidase in complex with l-lactate was solved at a 1.33 Å resolution. The electron density of the bound l-lactate was clearly shown and comparisons of the free form and substrate bound complexes demonstrated that l-lactate was bound to the FMN and an additional active site within the enzyme complex. l-lactate interacted with the related side chains, which play an important role in enzymatic catalysis and especially the coupled movement of H265 and D174, which may be essential to activity. These observations not only reveal the enzymatic mechanism for l-lactate binding but also demonstrate the dynamic motion of these enzyme structures in response to substrate binding and enzymatic reaction progression. PubMed: 34214876DOI: 10.1016/j.bbrc.2021.06.078 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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