7F22

L-lactate oxidase with pyruvate

7F22 の概要

• エントリーDOI: 10.2210/pdb7f22/pdb
• 分子名称: L-lactate oxidase, FLAVIN MONONUCLEOTIDE, PYRUVIC ACID, ... (4 entities in total)
• 機能のキーワード: pyruvate, complex, oxidoreductase
• 由来する生物種: Aerococcus viridans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 162225.44

構造登録者

Morimoto, Y.,Inaka, K. (登録日: 2021-06-10, 公開日: 2022-03-23, 最終更新日: 2023-11-29)

主引用文献

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

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: 34214876
DOI: 10.1016/j.bbrc.2021.06.078

実験手法

X-RAY DIFFRACTION (1.41 Å)