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

A putative precursor of isomalabaricane triterpenoids from lanosterol synthase mutants.

Organic letters - 2 Feb 2006

Lodeiro Silvia, Wilson William K, Shan Hui, Matsuda Seiichi P T

Abstract excerpt

[reaction: see text]. Known lanosterol synthase mutants produce monocyclic or tetracyclic byproducts from oxidosqualene. We describe Erg7 Tyr510 mutants that cause partial substrate misfolding and generate a tricyclic byproduct. This novel triterpene, (13alphaH)-isomalabarica-14(27),17E,21-trien-3beta-ol, is the likely biosynthetic precursor of isomalabaricane triterpenoids in sponges. The results suggest the...

Read the complete abstract on PubMed

Topics

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

Share to Biological Evolution
Share to Contraindications
Share to Intramolecular Transferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Structure

Share to Mutation

Share to Porifera

Share to Triterpenes

Source

Identifiers

PMID: 16435854
DOI: 10.1021/ol052725j

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

A putative precursor of isomalabaricane triterpenoids from lanosterol synthase mutants.PMID 16435854Read ↗

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

Importance of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase tyrosine 707 residue for chair-boat bicyclic ring formation and deprotonation reactions.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 ↗

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

Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae.Semantic proximity Read ↗

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

Protein engineering of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase into parkeol synthase.Semantic proximity Read ↗

Mechanistic insights into oxidosqualene cyclizations through homology modeling.Semantic proximity Read ↗

Directed evolution to generate cycloartenol synthase mutants that produce lanosterol.Semantic proximity Read ↗

Protein plasticity: a single amino acid substitution in the Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase generates protosta-13(17),24-dien-3beta-ol, a rearrangement product.Semantic proximity Read ↗

Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation.Semantic proximity Read ↗

Steric bulk at cycloartenol synthase position 481 influences cyclization and deprotonation.Semantic proximity Read ↗

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