Lupeol synthase

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Lupeol synthase
Identifiers
EC no. 5.4.99.41
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Lupeol synthase (EC 5.4.99.41, LUPI, BPW, RcLUS) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, lupeol-forming). [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

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

Also forms some beta-amyrin.

Related Research Articles

<span class="mw-page-title-main">Lanosterol synthase</span> Mammalian protein found in Homo sapiens

Lanosterol synthase is an oxidosqualene cyclase (OSC) enzyme that converts (S)-2,3-oxidosqualene to a protosterol cation and finally to lanosterol. Lanosterol is a key four-ringed intermediate in cholesterol biosynthesis. In humans, lanosterol synthase is encoded by the LSS gene.

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

Germanicol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualenee 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

Isomultiflorenol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualenee mutase . It catalyses the chemical reaction:

β-amyrin 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

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

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

References

  1. Herrera JB, Bartel B, Wilson WK, Matsuda SP (December 1998). "Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene". Phytochemistry. 49 (7): 1905–11. doi:10.1016/s0031-9422(98)00366-5. PMID   9883589.
  2. Shibuya M, Zhang H, Endo A, Shishikura K, Kushiro T, Ebizuka Y (November 1999). "Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases". European Journal of Biochemistry. 266 (1): 302–7. doi: 10.1046/j.1432-1327.1999.00875.x . PMID   10542078.
  3. Segura MJ, Meyer MM, Matsuda SP (July 2000). "Arabidopsis thaliana LUP1 converts oxidosqualene to multiple triterpene alcohols and a triterpene diol". Organic Letters. 2 (15): 2257–9. doi:10.1021/ol006016b. PMID   10930257.
  4. Zhang H, Shibuya M, Yokota S, Ebizuka Y (May 2003). "Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla var. japonica: molecular evolution of oxidosqualene cyclases in higher plants". Biological & Pharmaceutical Bulletin. 26 (5): 642–50. doi: 10.1248/bpb.26.642 . PMID   12736505.
  5. Hayashi H, Huang P, Takada S, Obinata M, Inoue K, Shibuya M, Ebizuka Y (July 2004). "Differential expression of three oxidosqualene cyclase mRNAs in Glycyrrhiza glabra". Biological & Pharmaceutical Bulletin. 27 (7): 1086–92. doi: 10.1248/bpb.27.1086 . PMID   15256745.
  6. Guhling O, Hobl B, Yeats T, Jetter R (April 2006). "Cloning and characterization of a lupeol synthase involved in the synthesis of epicuticular wax crystals on stem and hypocotyl surfaces of Ricinus communis". Archives of Biochemistry and Biophysics. 448 (1–2): 60–72. doi:10.1016/j.abb.2005.12.013. PMID   16445885.
  7. Basyuni M, Oku H, Tsujimoto E, Kinjo K, Baba S, Takara K (October 2007). "Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae". The FEBS Journal. 274 (19): 5028–42. doi: 10.1111/j.1742-4658.2007.06025.x . PMID   17803686.