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

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

Phytochemistry - 1 Oct 2026

Lin Pengyang, Wang Yunpeng, Li Bing, Zhang Xuebingting, Fan Baolian, Huang Ruoshi, Ji Zhongju, Zhang Fan, Liang Jingcai, Duan Lixin

Abstract excerpt

Protostadienol-type tetracyclic triterpenes, characterized by a rare chair-boat-chair (C-B-C) cyclized sterol-type backbone, serve as high-value pharmaceutical precursors due to their positionally isomeric double bonds. Plant derived-protostane triterpenoids have different skeletons at the double bond positions from fungal protostane triterpenoids. The characteristic mechanisms of double bond positions for the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Molecular Structure

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Triterpenes

Source

Identifiers

PMID: 42106134
DOI: 10.1016/j.phytochem.2026.114950

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single-site amino acid residue mutation reshapes the characteristics of double bond positions for protostadienol-type triterpenols.PMID 42106134Read ↗

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

Control of the 1,2-rearrangement process by oxidosqualene cyclases during triterpene biosynthesis.Semantic proximity Read ↗

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

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

Increasing complexity of a diterpene synthase reaction with a single residue switch.Semantic proximity Read ↗

Identification of key amino acid residues determining product specificity of 2,3-oxidosqualene cyclase in Oryza species.Semantic proximity Read ↗

The cysteine 703 to isoleucine or histidine mutation of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae generates an iridal-type triterpenoid.Semantic proximity Read ↗

Mutation of isoleucine 705 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae affects lanosterol's C/D-ring cyclization and 17α/β-exocyclic side chain stereochemistry.Semantic proximity Read ↗

Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis.Semantic proximity Read ↗

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

Enzymatic Plasticity Inspired by the Diterpene Cyclase CotB2.Semantic proximity Read ↗

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

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