These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Michael additions in polyketide biosynthesis.
    Author: Miyanaga A.
    Journal: Nat Prod Rep; 2019 Mar 20; 36(3):531-547. PubMed ID: 30311933.
    Abstract:
    Covering: up to July 2018 Polyketides constitute a large family of natural products exhibiting various biological activities. Polyketide biosynthetic systems employ several strategies for the production of structurally diverse polyketides. Among the polyketide biosynthetic enzymes, a growing number of enzymes that catalyze a Michael-type addition have been identified. These enzymes are responsible for constructing unique polyketide backbone structures, forming heterocycles, and incorporating heteroatoms into the polyketide backbone, all of which contribute to the diversification of the polyketide structure. This review summarizes the current understanding of the function of enzymes catalyzing a Michael-type addition in polyketide biosynthesis, with a particular focus on mechanistic studies.
    [Abstract] [Full Text] [Related] [New Search]