小分子与人类脯氨酰羟化酶共价反应——朝向活性调节和底物捕获。
Small-molecules that covalently react with a human prolyl hydroxylase - towards activity modulation and substrate capture.
机构信息
Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK.
出版信息
Chem Commun (Camb). 2019 Jan 22;55(8):1020-1023. doi: 10.1039/c8cc07706a.
Abstract
We describe covalently binding modulators of the activity of human prolyl hydroxylase domain 2 (PHD2) and studies towards a strategy for photocapture of PHD2 substrates. Reversible active site binding of electrophile bearing compounds enables susbsequent covalent reaction with a lysine residue (K408) in the flexible C-terminal region of PHD2 to give a modified protein that retains catalytic activity.
摘要
我们描述了人源脯氨酰羟化酶结构域 2（PHD2）活性的共价结合调节剂，以及用于 PH2 底物光捕获的策略的研究。带正电的化合物可逆地与活性位点结合，随后与 PHD2 柔性 C 末端区域的赖氨酸残基（K408）发生共价反应，得到保留催化活性的修饰蛋白。
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