the recombinant purified enzyme catalyses the synthesis of beta-sesquiphellandrene, not alpha-farnesene, GC-MS analysis of enzyme reaction products, overview. The major product is beta-sesquiphellandrene (KI:1516, about 97%) and beta-farnesene (about 3%) as a minor product
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
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
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recombinant His6-tagged enzyme PmSTS from Escherichia coli strain BL21(DE3), the recombinant enzyme has an N-terminal truncation, that dramatically improves the homogeneity of PmSTS during protein purification, suggesting that the disordered N-terminal region may have caused the formation of soluble aggregate