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• 54910-48-4 squalene 2,3(S)-oxide 

Relevant academic research and scientific papers

Alteration of the substrate's prefolded conformation and cyclization stereochemistry of oxidosqualene-lanosterol cyclase of saccharomyces cerevisiae by substitution at Phenylalanine 699

[Chemical equaction presented] The Saccharomyces cerevisiae ERG7 Phe699 mutants produced one chair-chair-chair (C-C-C) and two chair-boat-chair (C-B-C) truncated tricyclic compounds, one tetracyclic 17α-exocyclic unrearranged intermediate, and

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

The Cys703 to Ile or His mutation within Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase ERG7 (ERG7C703I/H) generates an unusual truncated bicyclic rearranged intermediate, (8R,9R,10R)-polypoda-5,13E, 17E,21-tetraen-3β-ol, related to iridal-skeleton triterpenoid. Numerous oxidosqualene-cyclized truncated intermediates, including tricyclic, unrearranged tetracyclic with 17α/β exocyclic hydrocarbon side chain, rearranged tetracyclic, and chair-chair-chair tricyclic intermediates (compounds 3-9), were also isolated from the ERG7C703X site-saturated mutations or the ERG7F699T/C703I double mutation, indicating the functional role of the Cys703 residue in stabilizing the bicyclic C-8 cation and the rearranged intermediate or interacting with Phe699, and opened a new avenue of engineering ERG7 for producing biological active agents.

Differential stereocontrolled formation of tricyclic triterpenes by mutation of tyrosine 99 of the oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae

The function of the Tyr99 residue from Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase (ERG7) was analyzed by constructing deletion, and site-saturated mutants. Two truncated intermediates, (13αH)- isomalabarica-14Z,17E,21-trien-3βol and. (13αH)