42998-52-7Relevant academic research and scientific papers
Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin
Li, Yuan,Zhang, Wan,Zhang, Hui,Tian, Wenya,Wu, Lian,Wang, Shuwen,Zheng, Mengmeng,Zhang, Jinru,Sun, Chenghai,Deng, Zixin,Sun, Yuhui,Qu, Xudong,Zhou, Jiahai
, p. 5823 - 5827 (2018)
Polyketides are a large family of pharmaceutically important natural products, and the structural modification of their scaffolds is significant for drug development. Herein, we report high-resolution X-ray crystal structures of the broadly selective acyltransferase (AT) from the splenocin polyketide synthase (SpnD-AT) in the apo form and in complex with benzylmalonyl and pentynylmalonyl extender unit mimics. These structures revealed the molecular basis for the stereoselectivity and substrate specificity of SpnD-AT, and enabled the engineering of the industrially important Ery-AT6 to broaden its substrate scope to include three new types of extender units.
