Type I PKSs are large, complex protein structures with multiple modules which in turn consist of several domains that are usually covalently connected to each other and fulfill different catalytic steps.

2019年2月20日 · Polyketides are constructed from simple carboxylic acid-derived components, often by filamentous bacteria using modular type I polyketide synthases (PKSs), gigantic protein complexes that house...

Polyketides constitute one of the largest families of natural products and many are biosynthesized by noniterative type I polyketide synthases (PKSs). Type I PKSs are multifunctional enzymes organized into modules, each of which harbors a set of distinct domains responsible for the catalysis of one cycle of polyketide chain elongation.

聚酮合酶(polyketide synthases,PKSs)是完成种类繁多的PKs生物合成的核心催化机器,具有严密、精巧的通用构造和普遍遵循且高效的基本流程,主要通过催化短链的羧酸衍生单元发生的连续的缩合反应来合成PKs,该过程与脂肪酸的生物合成极为相似[1]。

2003年2月21日 · Type I polyketide synthases (PKSs) are multifunctional enzymes that are organized into modules, each of which minimally contains a β-ketoacyl synthase, an acyltransferase (AT), and an acyl carrier protein.

Abstract: Most polyketide natural compounds, such as antibiotics, antineoplastics and immunosuppressants, are produced by type Ⅰ polyketide synthases (PKSs). Type Ⅰ PKSs are composed of several catalytic modules, each of which contains iterative domains, such as acyltransferase (AT) domain, for one round of polyketide chain elongation.

2024年6月25日 · Modular Type I Cis-AT polyketides (MT1PK) are a major subtype of polyketides, mainly produced by bacteria. They include antibiotics such as rifamycin 12, antifungals...

2020年3月26日 · Type I polyketide synthases (T1PKSs) are one of the most extensively studied PKSs, which can act either iteratively or via an assembly-line mechanism. Domains in the T1PKSs can readily be predicted by computational tools …

2023年9月26日 · 科研人员正迫切期待着进一步理解type I iPKSs，最终创造具备可编程功能的分子机器，产生个性化、定制化的终产物与新型药物。 该研究得到了国家重点研究发展计划、国家自然科学基金、国家博士后科学基金以及上海市超级博士后激励计划的经费支持。

2020年3月27日 · We demonstrate that JamABC works as a trans loading system for engineered type I PKSs to produce alkyne-tagged polyketides. In addition, the production efficiency can be improved by enhancing the interactions between the carrier protein (JamC) and PKSs using docking domains and site-directed mutagenesis of JamC.