Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Systematic identification of functional residues of Artemisia annua amorpha-4,11-diene synthase.

The Biochemical journal - 16 Jun 2017

Fang Xin, Li Jian-Xu, Huang Jin-Quan, Xiao You-Li, Zhang Peng, Chen Xiao-Ya

Abstract excerpt

Terpene synthases (TPSs) are responsible for the extremely diversified and complex structure of terpenoids. Amorpha-4,11-diene synthase (ADS) has a high (90%) fidelity in generating the sesquiterpene precursor for the biosynthesis of artemisinin, an antimalarial drug, however, little is known about how active site residues of ADS are involved in carbocation rearrangement and cyclization reactions. Here, we...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alkyl and Aryl Transferases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Conformation

Share to Sesquiterpenes

Source

Identifiers

PMID: 28526743
DOI: 10.1042/BCJ20170060

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Systematic identification of functional residues of Artemisia annua amorpha-4,11-diene synthase.PMID 28526743Read ↗

Biosynthetic potential of sesquiterpene synthases: product profiles of Egyptian Henbane premnaspirodiene synthase and related mutants.Semantic proximity Read ↗

Comparative functional analysis of CYP71AV1 natural variants reveals an important residue for the successive oxidation of amorpha-4,11-diene.Semantic proximity Read ↗

A conserved amino acid residue critical for product and substrate specificity in plant triterpene synthases.Semantic proximity Read ↗

Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum.Semantic proximity Read ↗

Functional Characterization and Mutagenesis Studies of a Microbial-like Diterpene Synthase from Huperzia serrata.Semantic proximity Read ↗

Production of amorphadiene in yeast, and its conversion to dihydroartemisinic acid, precursor to the antimalarial agent artemisinin.Semantic proximity Read ↗

Rational conversion of substrate and product specificity in a Salvia monoterpene synthase: structural insights into the evolution of terpene synthase function.Semantic proximity Read ↗

Mechanism-Based Post-Translational Modification and Inactivation in Terpene Synthases.Semantic proximity Read ↗

Artemisia annua mutant impaired in artemisinin synthesis demonstrates importance of nonenzymatic conversion in terpenoid metabolism.Semantic proximity Read ↗

Single-site amino acid residue mutation reshapes the characteristics of double bond positions for protostadienol-type triterpenols.Semantic proximity Read ↗

Unearthing a sesterterpene biosynthetic repertoire in the Brassicaceae through genome mining reveals convergent evolution.Semantic proximity Read ↗

Functional characterization of sesquiterpene synthase from Polygonum minus.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.