| Entry |
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| Name |
alpha-seco-amyrin synthase
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| Class |
Isomerases;
Intramolecular transferases;
Transferring other groups
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| Sysname |
(3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, alpha-seco-amyrin-forming)
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| Reaction(IUBMB) |
(3S)-2,3-epoxy-2,3-dihydrosqualene = alpha-seco-amyrin [RN: R09912]
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| Reaction(KEGG) |
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| Substrate |
(3S)-2,3-epoxy-2,3-dihydrosqualene [CPD: C01054]
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| Product |
alpha-seco-amyrin [CPD: C20191]
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| Comment |
The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of alpha- and beta-seco-amyrin. See EC 5.4.99.54, beta-seco-amyrin synthase.
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| Pathway |
| Sesquiterpenoid and triterpenoid biosynthesis |
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| Orthology |
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| Genes |
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| Reference |
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| Authors |
Shibuya M, Xiang T, Katsube Y, Otsuka M, Zhang H, Ebizuka Y |
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| Title |
Origin of structural diversity in natural triterpenes: direct synthesis of seco-triterpene skeletons by oxidosqualene cyclase. |
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| Journal |
J. Am. Chem. Soc. 129 (2007) 1450-5. |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |
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