Download MendeleyDynamic 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.(2021) Biochem Biophys Res Commun 568: 131-135
- PubMed: 34214876
- DOI: https://doi.org/10.1016/j.bbrc.2021.06.078
- Primary Citation of Related Structures:
7F1Y, 7F20, 7F21, 7F22 - PubMed Abstract:
The crystal structure of l-lactate oxidase in complex with l-lactate was solved at a 1.33?? 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.
Organizational Affiliation:
MARUWA Foods and Biosciences, Inc., 170-1, Tsutsui-cho, Yamatokoriyama, Nara, 639-1123, Japan.
