Unknown

Dataset Information

0

Identification and characterization of a novel sesquiterpene synthase, 4-amorphen-11-ol synthase, from Artemisia maritima.


ABSTRACT: Artemisinin, a sesquiterpene lactone exhibiting effective antimalarial activity, is produced by only Artemisia annua plant. A key step in artemisinin biosynthesis is the cyclization of farnesyl pyrophosphate (FPP) to amorpha-4,11-diene catalyzed by amorpha-4,11-diene synthase (AaADS). Intriguingly, several non-artemisinin-producing Artemisia plants also express genes highly homologous to AaADS. Our previous functional analysis of these homologous enzymes revealed that they catalyzed the synthesis of rare natural sesquiterpenoids. In this study, we analyzed the function of another putative sesquiterpene synthase highly homologous to AaADS from A. maritima. Unlike AaADS, in vivo enzymatic assay showed that this enzyme cyclized FPP to 4-amorphen-11-ol, a precursor of several gastroprotective agents. The discovery of 4-amorphen-11-ol synthase (AmAOS) and the successful de novo production of 4-amorphen-11-ol in engineered yeast demonstrated herein provides insights into the methods used to enhance its production for future application.

SUBMITTER: Muangphrom P 

PROVIDER: S-EPMC6879386 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Identification and characterization of a novel sesquiterpene synthase, 4-amorphen-11-ol synthase, from <i>Artemisia maritima</i>.

Muangphrom Paskorn P   Seki Hikaru H   Matsumoto Seiya S   Nishiwaki Mika M   Fukushima Ery O EO   Muranaka Toshiya T  

Plant biotechnology (Tokyo, Japan) 20180601 2


Artemisinin, a sesquiterpene lactone exhibiting effective antimalarial activity, is produced by only <i>Artemisia annua</i> plant. A key step in artemisinin biosynthesis is the cyclization of farnesyl pyrophosphate (FPP) to amorpha-4,11-diene catalyzed by amorpha-4,11-diene synthase (AaADS). Intriguingly, several non-artemisinin-producing <i>Artemisia</i> plants also express genes highly homologous to <i>AaADS</i>. Our previous functional analysis of these homologous enzymes revealed that they c  ...[more]

Similar Datasets

| S-EPMC7866031 | biostudies-literature
| S-EPMC3151043 | biostudies-literature
| S-EPMC2951637 | biostudies-literature
| S-EPMC3942395 | biostudies-literature
| PRJNA179006 | ENA
| PRJNA178759 | ENA
| S-EPMC7886051 | biostudies-literature
| S-EPMC5668897 | biostudies-literature
| S-EPMC1652817 | biostudies-literature
| S-EPMC4426440 | biostudies-literature