Scholarlink

Background <p>The biosynthesis of bacterial aromatic polyketides (type II polyketides, T2PKs) employs a single set of catalysts (ketosynthases, KSs or KS<sub>α</sub>, with chain length factors, CLFs or KS<sub>β</sub>) and iteratively assembles a carbon backbone with precise chain length control. Considering the increasing number of T2PKs discovered in laboratory settings, it is necessary to understand the evolutionary trajectories of KSs and CLFs.</p> Results <p>We employ our recently developed algorithm, MAAPE, based on large protein language model to glean insights into the evolution process of KSs and CLFs. Our findings indicate the evolutionary history of KS and CLF domains from bacterial T2PKSs and identify a shared ancestral cluster (Cluster A), supporting a common origin. Despite structural homology, KSs and CLFs followed distinct evolutionary paths, shaped by coevolution and early horizontal gene transfer.</p> Conclusions <p>Understanding the evolutionary lineage of these enzymes will illuminate the natural optimization processes of their functions and present opportunities for the rational design of novel polyketides with enhanced efficacy.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

The evolutionary processes of bacterial aromatic polyketide ketosynthases

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年7月25日

查看全文
  • Xiaoyu Wang,
  • Qiandi Gao,
  • Liangjun Ge,
  • Zhiwei Qin

摘要

Background

The biosynthesis of bacterial aromatic polyketides (type II polyketides, T2PKs) employs a single set of catalysts (ketosynthases, KSs or KSα, with chain length factors, CLFs or KSβ) and iteratively assembles a carbon backbone with precise chain length control. Considering the increasing number of T2PKs discovered in laboratory settings, it is necessary to understand the evolutionary trajectories of KSs and CLFs.

Results

We employ our recently developed algorithm, MAAPE, based on large protein language model to glean insights into the evolution process of KSs and CLFs. Our findings indicate the evolutionary history of KS and CLF domains from bacterial T2PKSs and identify a shared ancestral cluster (Cluster A), supporting a common origin. Despite structural homology, KSs and CLFs followed distinct evolutionary paths, shaped by coevolution and early horizontal gene transfer.

Conclusions

Understanding the evolutionary lineage of these enzymes will illuminate the natural optimization processes of their functions and present opportunities for the rational design of novel polyketides with enhanced efficacy.