Exploring the compatibility of phosphopantetheinyl transferases with acyl carrier proteins spanning type II polyketide synthase sequence space.

ABSTRACT: Phosphopantetheinyl transferases (PPTases) play an essential role in primary and secondary metabolism. These enzymes facilitate the posttranslational activation of acyl carrier proteins (ACPs) central to the biosynthesis of fatty acids and polyketides. Modulation of ACP-PPTase interactions is a promising approach to both increase access to desired molecular outputs and disrupt mechanisms associated with disease progression. However, such an approach requires understanding the molecular principles that govern ACP-PPTase interactions across diverse synthases. Through a multiyear, course-based undergraduate research experience (CURE), 17 ACPs representing a range of putative type II polyketide synthases, from actinobacterial and nonactinobacterial phyla, were evaluated as substrates for three

SUBMITTER: Bifendeh ALN 

PROVIDER: S-EPMC12551638 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature