MARUWA Foods and Biosciences, Inc., 170-1, Tsutsui-cho, Yamatokoriyama, Nara, 639-1123, Japan.
AICHI SR Center, Nagoya University, Nagoya, Aichi, 464-8603, Japan.
Biochem Biophys Res Commun. 2021 Sep 3;568:131-135. doi: 10.1016/j.bbrc.2021.06.078. Epub 2021 Jun 30.
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.
l-乳酸氧化酶与 l-乳酸复合物的晶体结构解析至 1.33Å 分辨率。结合的 l-乳酸的电子密度清晰可见，游离形式和底物结合复合物的比较表明，l-乳酸与 FMN 和酶复合物中的另一个活性位点结合。l-乳酸与相关侧链相互作用，这些侧链在酶催化中起着重要作用，特别是 H265 和 D174 的偶联运动，这对活性可能是必不可少的。这些观察结果不仅揭示了 l-乳酸结合的酶机制，还证明了这些酶结构在底物结合和酶反应进展过程中的动态运动。
