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Literature summary extracted from

  • Taramino, S.; Valachovic, M.; Oliaro-Bosso, S.; Viola, F.; Teske, B.; Bard, M.; Balliano, G.
    Interactions of oxidosqualene cyclase (Erg7p) with 3-keto reductase (Erg27p) and other enzymes of sterol biosynthesis in yeast (2010), Biochim. Biophys. Acta, 1801, 156-162.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.270 Saccharomyces cerevisiae
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-
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5.4.99.7 Saccharomyces cerevisiae
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-
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5.4.99.7 Saccharomyces cerevisiae STY2
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.7 (3S)-2,3-oxidosqualene
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 Saccharomyces cerevisiae lanosterol
-
 ?
5.4.99.7 (3S)-2,3-oxidosqualene
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 Saccharomyces cerevisiae STY2 lanosterol
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 ?
5.4.99.7 dioxidosqualene
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 Saccharomyces cerevisiae 24(S),25-epoxylanosterol
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 ?
5.4.99.7 dioxidosqualene
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 Saccharomyces cerevisiae STY2 24(S),25-epoxylanosterol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.4.99.7 ERG7
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 Saccharomyces cerevisiae
5.4.99.7 Erg7p
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 Saccharomyces cerevisiae
5.4.99.7 OSC
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 Saccharomyces cerevisiae
5.4.99.7 Oxidosqualene cyclase
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 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
1.1.1.270 physiological function loss of the 3-keto reductase also results in a concomitant loss of activity of the upstream oxidosqualene cyclase. Oxidosqualene cyclase is not required for the 3-ketoreductase activity. In Saccharomyces cerevisiae, the protective relationship between the 3-keto reductase Erg27 and oxidosqualene cyclase Erg7p is not reciprocal Saccharomyces cerevisiae