LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 2 of total 2

Search options

  1. Article ; Online: Characterization of three succinyl-CoA acyltransferases involved in polyketide chain assembly

    Liu, Lilu / Wang, Wenzhao / Chen, Meng / Zhang, Yuwei / Mao, Huijin / Wang, Dacheng / Chen, Yihua / Li, Pengwei

    Appl Microbiol Biotechnol. 2023 Apr., v. 107, no. 7-8 p.2403-2412

    2023  

    Abstract: Polyketides are a class of natural products with astonishing structural diversities, fascinating biological activities, and a versatile of applications. In polyketides biosynthesis, acyltransferases (ATs) are the ‘gatekeeping’ enzymes selecting the ... ...

    Abstract Polyketides are a class of natural products with astonishing structural diversities, fascinating biological activities, and a versatile of applications. In polyketides biosynthesis, acyltransferases (ATs) are the ‘gatekeeping’ enzymes selecting the specific CoA-activated acyl groups as building blocks and transferring them onto the phosphopantetheine arm of acyl carrier proteins (ACPs) to enable the following condensation reactions to assemble the polyketide chain. Herein, the Art2 protein from aurantinins, a group of the antibacterial polyketides, is characterized in vitro as an AT that can load a CoA-activated succinyl unit onto the first ACP domain of Art17 (ACPAᵣₜ₁₇₋₁). In addition, another two proteins, GbnB and EtnB, involved in the biosynthesis of gladiolin and etnangien respectively, were traced by literature mining, homologous searching, and product structure analysis and then identified as functional succinyl-CoA ATs by the ACPAᵣₜ₁₇₋₁ assays. Taken together, by the assay method employing ACPAᵣₜ₁₇₋₁ as an acyl acceptor, we identified three ATs that can introduce a succinyl unit into the polyketide assembly line, which enriches the toolbox of polyketide biosynthetic enzymes and sets a stage for incorporating a succinyl unit into polyketide backbones in synthetic biological manners. KEY POINTS: • Three acyltransferases that are able to load ACP with a succinyl unit were characterized in vitro. • ACPAᵣₜ₁₇₋₁ can be used as an acceptor to assay succinyl-CoA AT from different polyketides. • The succinyl unit can be incorporated into polyketides assembly process.
    Keywords acyltransferases ; biosynthesis ; polyketides
    Language English
    Dates of publication 2023-04
    Size p. 2403-2412.
    Publishing place Springer Berlin Heidelberg
    Document type Article ; Online
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-023-12481-9
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

  2. Article ; Online: Characterization of three succinyl-CoA acyltransferases involved in polyketide chain assembly.

    Liu, Lilu / Wang, Wenzhao / Chen, Meng / Zhang, Yuwei / Mao, Huijin / Wang, Dacheng / Chen, Yihua / Li, Pengwei

    Applied microbiology and biotechnology

    2023  Volume 107, Issue 7-8, Page(s) 2403–2412

    Abstract: Polyketides are a class of natural products with astonishing structural diversities, fascinating biological activities, and a versatile of applications. In polyketides biosynthesis, acyltransferases (ATs) are the 'gatekeeping' enzymes selecting the ... ...

    Abstract Polyketides are a class of natural products with astonishing structural diversities, fascinating biological activities, and a versatile of applications. In polyketides biosynthesis, acyltransferases (ATs) are the 'gatekeeping' enzymes selecting the specific CoA-activated acyl groups as building blocks and transferring them onto the phosphopantetheine arm of acyl carrier proteins (ACPs) to enable the following condensation reactions to assemble the polyketide chain. Herein, the Art2 protein from aurantinins, a group of the antibacterial polyketides, is characterized in vitro as an AT that can load a CoA-activated succinyl unit onto the first ACP domain of Art17 (ACP
    MeSH term(s) Acyltransferases/metabolism ; Polyketides/metabolism ; Acyl Coenzyme A/metabolism ; Anti-Bacterial Agents ; Polyketide Synthases/metabolism
    Chemical Substances succinyl-coenzyme A (BSI27HW5EQ) ; Acyltransferases (EC 2.3.-) ; Polyketides ; Acyl Coenzyme A ; Anti-Bacterial Agents ; Polyketide Synthases (79956-01-7)
    Language English
    Publishing date 2023-03-16
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-023-12481-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top