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Literature summary for 5.4.99.7 extracted from

  • Wu, T.K.; Chang, C.H.
    Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae (2004), ChemBioChem, 5, 1712-1715.
    View publication on PubMed
Search for more literature for 5.4.99.7

Cloned(Commentary)

Cloned (Comment) Organism
-
 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
V454A results in the production of an additional truncated monocyclic achilleol A Saccharomyces cerevisiae
V454G results in the production of an additional truncated monocyclic achilleol A Saccharomyces cerevisiae
Y510A produces lanosterol, parkeol and achilleol A in a 39:34:27 ratio Saccharomyces cerevisiae
Y510K fails to maintain cell viability in the absence of ergosterol, in the presence of ergosterol the mutant produces achilleol A and camelliol C in a ratio of 86:14 Saccharomyces cerevisiae
Y510W fails to maintain cell viability in the absence of ergosterol, in the presence of ergosterol the mutant produces achilleol A and camelliol C in a ratio of 96:4 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(3S)-2,3-oxidosqualene Saccharomyces cerevisiae
-
 lanosterol
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-2,3-oxidosqualene
-
 Saccharomyces cerevisiae lanosterol
-
 ?

Synonyms

Synonyms Comment Organism
ERG7
-
 Saccharomyces cerevisiae
Oxidosqualene-lanosterol cyclase
-
 Saccharomyces cerevisiae