4.2.3.123: beta-sesquiphellandrene synthase
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For detailed information about beta-sesquiphellandrene synthase, go to the full flat file.
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Synonyms
Os08g07100, PmSTS, STS, TPS1
ECTree
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General Information
General Information on EC 4.2.3.123 - beta-sesquiphellandrene synthase
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evolution
the enzyme belongs to the sesquiterpene synthases, it contains the NSE/DTE motif commonly found in terpene synthases
physiological function
generation of transgenic Arabiopsis thaliana by Agrobacterium-mediated overexpression. Transgenic plants have long hypocotyls, green leaves, and long main roots with the formation of lateral roots. In contrast, the nontransformants show short hypocotyls, bleached out leaves, and no lateral root formation. Transgenic plants show delayed growth, smaller basal rosette leaves and shorter and fewer flowering stems and fewer seeds, compared to the wild-type
additional information
homology model of PmSTS shows the structure domain and active site of the enzyme using the structures of monoterpene synthase Salvia officinalis (+)-bornyl diphosphate synthase (PDB ID 1N20) and Mentha spicata 4S-limonene synthase (PDB ID 2ONG), and sesquiterpene Nicotiana tabacum 5-epi-aristolochene synthase (PDB ID 3M01), Gossypium arboreum beta-cadinene synthase (PDB ID 3G4F) and Artemisia annua alpha-bisabolol synthase (PDB ID 4FJQ). The homology structure of PmSTS that allows good fitting of a substrate analogue into the catalytic active site suggests that PmSTS may adopt a sesquiterpene biosynthesis mechanism similar to other plant sesquiterpene synthases
additional information
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homology model of PmSTS shows the structure domain and active site of the enzyme using the structures of monoterpene synthase Salvia officinalis (+)-bornyl diphosphate synthase (PDB ID 1N20) and Mentha spicata 4S-limonene synthase (PDB ID 2ONG), and sesquiterpene Nicotiana tabacum 5-epi-aristolochene synthase (PDB ID 3M01), Gossypium arboreum beta-cadinene synthase (PDB ID 3G4F) and Artemisia annua alpha-bisabolol synthase (PDB ID 4FJQ). The homology structure of PmSTS that allows good fitting of a substrate analogue into the catalytic active site suggests that PmSTS may adopt a sesquiterpene biosynthesis mechanism similar to other plant sesquiterpene synthases