Department of Chemistry, City University of Hong Kong, Tat Chee Avenue, Kowloon, Hong Kong SAR, China.
Small Methods. 2024 Nov;8(11):e2400107. doi: 10.1002/smtd.202400107. Epub 2024 Apr 21.
A comparison of substrate-binding site amino acid residues in the C-methyltransferase (MT) domains of fungal nonreducing polyketide synthases (NR-PKSs) suggests that these residues are correlated with the methylation modes used by the PKSs. A PKS, designated as AsbPKS, with substrate-binding site residues distinct from those of other known PKSs is focused on. The characterization of AsbPKS revealed that it yields an isocoumarin derivative, anhydrosclerotinin B (1), the biosynthesis of which involves a previously unreported methylation pattern. This study demonstrates the utility of MT domain-focused genome mining for the discovery of PKSs with new functions.
真菌非还原型聚酮合酶（NR-PKS）的 C-甲基转移酶（MT）结构域中底物结合位点的氨基酸残基比较表明，这些残基与 PKS 所使用的甲基化模式相关。我们关注了一个具有独特底物结合位点残基的 PKS，称为 AsbPKS。AsbPKS 的特征表明，它产生了一种异香豆素衍生物，无水硬脂菌素 B（1），其生物合成涉及以前未报道的甲基化模式。本研究证明了专注于 MT 结构域的基因组挖掘在发现具有新功能的 PKS 方面的实用性。
