7f1y
From Proteopedia
L-lactate oxidase without substrate
Structural highlights
FunctionLOX_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 PubMedThe crystal structure of l-lactate oxidase in complex with l-lactate was solved at a 1.33 A 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. Dynamic interactions in the l-lactate oxidase active site facilitate substrate binding at pH4.5.,Furubayashi N, Inaka K, Kamo M, Umena Y, Matsuoka T, Morimoto Y Biochem Biophys Res Commun. 2021 Sep 3;568:131-135. doi:, 10.1016/j.bbrc.2021.06.078. Epub 2021 Jun 30. PMID:34214876[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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