Center for Integrated Protein Science Munich (CIPSM), Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching (Germany).
Angew Chem Int Ed Engl. 2014 Jul 28;53(31):8150-3. doi: 10.1002/anie.201402595. Epub 2014 Jun 10.
The dehydrogenase PylD catalyzes the ultimate step of the pyrrolysine pathway by converting the isopeptide L-lysine-Nε-3R-methyl-D-ornithine to the 22nd proteinogenic amino acid. In this study, we demonstrate how PylD can be harnessed to oxidize various isopeptides to novel amino acids by combining chemical synthesis with enzyme kinetics and X-ray crystallography. The data enable a detailed description of the PylD reaction trajectory for the biosynthesis of pyrroline and tetrahydropyridine rings as constituents of pyrrolysine analogues.
脱氢酶 PylD 通过将异肽 L-赖氨酸-Nε-3R-甲基-D-鸟氨酸转化为第 22 种蛋白质氨基酸,催化吡咯赖氨酸途径的最后一步。在这项研究中,我们通过化学合成与酶动力学和 X 射线晶体学相结合,展示了如何利用 PylD 将各种异肽氧化为新型氨基酸。这些数据能够详细描述 PylD 反应轨迹,用于合成吡咯啉和四氢吡啶环,作为吡咯赖氨酸类似物的组成部分。