Baruol synthase

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Baruol synthase
Identifiers
EC no. 5.4.99.57
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Baruol synthase (EC 5.4.99.57, BARS1) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baruol-forming). [1] This enzyme catalyses the following chemical reaction

(3S)-2,3-epoxy-2,3-dihydrosqualene baruol

The enzyme from Arabidopsis thaliana also produces traces of 22 other triterpenoids.

Related Research Articles

Arabidiol synthase (EC 4.2.1.124, PEN1 (gene), (S)-squalene-2,3-epoxide hydro-lyase (arabidiol forming)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene hydro-lyase (arabidiol forming). This enzyme catalyses the following chemical reaction

Dammarenediol II synthase (EC 4.2.1.125, dammarenediol synthase, 2,3-oxidosqualene (20S)-dammarenediol cyclase, DDS, (S)-squalene-2,3-epoxide hydro-lyase (dammarenediol-II forming)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene hydro-lyase (dammarenediol-II forming). This enzyme catalyses the following chemical reaction

Lupan-3β,20-diol synthase (EC 4.2.1.128, LUP1 (gene)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene hydro-lyase (lupan-3beta,20-diol forming). This enzyme catalyses the following chemical reaction

Thalianol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Protostadienol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Cucurbitadienol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Taraxerol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Camelliol C synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

α-Amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Shionone synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Parkeol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Achilleol B synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Glutinol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Friedelin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Baccharis oxide synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

α-seco-amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Marneral synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase. This enzyme catalyses the following chemical reaction

β-seco-amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

δ-Amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Tirucalladienol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

References

  1. Lodeiro S, Xiong Q, Wilson WK, Kolesnikova MD, Onak CS, Matsuda SP (September 2007). "An oxidosqualene cyclase makes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis". Journal of the American Chemical Society. 129 (36): 11213–22. doi:10.1021/ja073133u. PMID   17705488.