β-amyrin synthase (EC 5.4.99.39, 2,3-oxidosqualene beta-amyrin cyclase, AsbAS1, BPY, EtAS, GgbAS1, LjAMY1, MtAMY1, PNY, BgbAS) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, beta-amyrin-forming).[1][2][3][4][5][6][7][8][9][10][11] This enzyme catalyses the following chemical reaction
| β-Amyrin synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.39 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- (3S)-2,3-epoxy-2,3-dihydrosqualene beta-amyrin
Some organism possess a monofunctional beta-amyrin synthase.
References
edit- ^ Abe I, Ebizuka Y, Seo S, Sankawa U (1989). "Purification of squalene-2,3-epoxide cyclases from cell suspension cultures of Rabdosia japonica Hara". FEBS Lett. 249: 100–104. doi:10.1016/0014-5793(89)80024-9. S2CID 84003375.
- ^ Abe I, Sankawa U, Ebizuka Y (1989). "Purification of 2,3-oxdosqualene:β-amyrin cyclase from pea seedlings". Chem. Pharm. Bull. 37: 536–. doi:10.1248/cpb.37.536.
- ^ Kushiro T, Shibuya M, Ebizuka Y (August 1998). "Beta-amyrin synthase--cloning of oxidosqualene cyclase that catalyzes the formation of the most popular triterpene among higher plants". European Journal of Biochemistry. 256 (1): 238–44. doi:10.1046/j.1432-1327.1998.2560238.x. PMID 9746369.
- ^ Hayashi H, Huang P, Kirakosyan A, Inoue K, Hiraoka N, Ikeshiro Y, Kushiro T, Shibuya M, Ebizuka Y (August 2001). "Cloning and characterization of a cDNA encoding beta-amyrin synthase involved in glycyrrhizin and soyasaponin biosyntheses in licorice". Biological & Pharmaceutical Bulletin. 24 (8): 912–6. doi:10.1248/bpb.24.912. PMID 11510484.
- ^ Husselstein-Muller T, Schaller H, Benveniste P (January 2001). "Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana". Plant Molecular Biology. 45 (1): 75–92. doi:10.1023/A:1006476123930. PMID 11247608. S2CID 20346811.
- ^ Iturbe-Ormaetxe I, Haralampidis K, Papadopoulou K, Osbourn AE (March 2003). "Molecular cloning and characterization of triterpene synthases from Medicago truncatula and Lotus japonicus". Plant Molecular Biology. 51 (5): 731–43. doi:10.1023/a:1022519709298. PMID 12683345. S2CID 33111263.
- ^ 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.
- ^ 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.
- ^ Kajikawa M, Yamato KT, Fukuzawa H, Sakai Y, Uchida H, Ohyama K (August 2005). "Cloning and characterization of a cDNA encoding beta-amyrin synthase from petroleum plant Euphorbia tirucalli L". Phytochemistry. 66 (15): 1759–66. doi:10.1016/j.phytochem.2005.05.021. PMID 16005035.
- ^ 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.
- ^ Liu Y, Cai Y, Zhao Z, Wang J, Li J, Xin W, Xia G, Xiang F (May 2009). "Cloning and Functional Analysis of a beta-amyrin synthase gene associated with oleanolic acid biosynthesis in Gentiana straminea MAXIM". Biological & Pharmaceutical Bulletin. 32 (5): 818–24. doi:10.1248/bpb.32.818. PMID 19420748.
External links
edit- Beta-amyrin+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
