4.2.3.104: alpha-humulene synthase
This is an abbreviated version!
For detailed information about alpha-humulene synthase, go to the full flat file.
Word Map on EC 4.2.3.104
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4.2.3.104
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ginger
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terpenoids
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mevalonate
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shampoo
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germacrene
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synthesis
- 4.2.3.104
- ginger
-
terpenoids
- mevalonate
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shampoo
- germacrene
- synthesis
Reaction
Synonyms
(E)-beta-caryophyllene/alpha-humulene synthase, alpha-humulene synthase, beta-caryophyllene/alpha-humulene synthase, CAHS, Hs1, Hs2, HS3, hum, sesquiterpene synthase1, Sst1, TPS1, TPS12, TPS2, ZSS1, zssI
ECTree
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General Information
General Information on EC 4.2.3.104 - alpha-humulene synthase
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metabolism
physiological function
additional information
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alpha-humulene synthase is a key enzyme of zerumbone biosynthesis
metabolism
the enzyme is involved in the biosynthetic pathways for sesquiterpenes found in agarwood and cell suspension cultures, putative pathway, overview. Various post-transcriptional, translational, or post-translational regulatory mechanisms affecting the expression or activity of alpha-humulene and delta-guaiene synthases are possible
metabolism
the enzyme is involved in the zerumbone biosynthesis in Zingiber zerumbet, proposed pathway and mechanism, overview
after tobacco rattlevirus-based virus induced gene silencing, beta-elemene, guaia-1(5),11-diene and guaia-1(10),11-diene are undetectable in suppressed leaves
physiological function
alpha-humulene is a common sesquiterpene widely distributed in plants, the synthase from Zingiber zerumbet is the only known sesquiterpene synthase to date catalyzing the formation of alpha-humulene as major product
sesquiterpene synthase alpha-humulene synthase (HUM) from Zingiber zerumbet is investigated for the bioconversion of the monoterpene precursors geranyl diphosphate (2E-GPP) and neryl diphosphate (2Z-NPP) as well as for the sesquiterpene precursor farnesyl diphosphate (2E,6E-FPP)
additional information
the enzyme contains conserved RPx8W motif and DDxxD motif, which is a divalent metal-ion substrate-binding site
additional information
the enzyme contains conserved RPx8W motif and DDxxD motif, which is a divalent metal-ion substrate-binding site
additional information
the enzyme contains conserved RPx8W motif and DDxxD motif, which is a divalent metal-ion substrate-binding site