Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Chembiochem. 2020 Nov 2;21(21):3077-3081. doi: 10.1002/cbic.202000306. Epub 2020 Jul 17.
We have examined the potential of the noncanonical amino acid (8-hydroxyquinolin-3-yl)alanine (HQAla) for the design of artificial metalloenzymes. HQAla, a versatile chelator of late transition metals, was introduced into the lactococcal multidrug-resistance regulator (LmrR) by stop codon suppression methodology. LmrR_HQAla was shown to complex efficiently with three different metal ions, Cu , Zn and Rh to form unique artificial metalloenzymes. The catalytic potential of the Cu -bound LmrR_HQAla enzyme was shown through its ability to catalyse asymmetric Friedel-Craft alkylation and water addition, whereas the Zn -coupled enzyme was shown to mimic natural Zn hydrolase activity.
我们研究了非典型氨基酸（8-羟基喹啉-3-基）丙氨酸（HQAla）在设计人工金属酶方面的潜力。HQAla 是一种多功能的后过渡金属螯合剂，通过终止密码子抑制方法被引入乳球菌多药耐药调节剂（LmrR）。结果表明，LmrR_HQAla 可以有效地与三种不同的金属离子 Cu 、 Zn 和 Rh 配位，形成独特的人工金属酶。Cu 结合的 LmrR_HQAla 酶的催化潜力通过其催化不对称傅-克烷基化和水加成反应的能力得到证明，而 Zn 偶联的酶则模拟了天然 Zn 水解酶的活性。
