深入研究过渡金属阳离子抑制 - 腺嘌呤 - L - 同型半胱氨酸水解酶的分子机制。
A closer look at molecular mechanisms underlying inhibition of -adenosyl-L-homocysteine hydrolase by transition metal cations.
机构信息
Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznan, Poland.
Provincial Sanitary-Epidemiological Station in Bialystok, Legionowa 8, 15-099, Bialystok, Poland.
出版信息
Chem Commun (Camb). 2024 Oct 8;60(81):11504-11507. doi: 10.1039/d4cc03143a.
We report biochemical and structural studies on inhibiting bacterial -adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor.
我们报告了关于过渡金属阳离子抑制细菌 -腺嘌呤-L-同型半胱氨酸水解酶的生化和结构研究。我们的结果揭示了酶失活的不同分子机制。根据阳离子的不同，该机制基于将酶固定在其关闭的、无活性的构象中，在活性位点内形成二硫键，或氧化辅因子的中间形式。
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