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1 o known conifer bifunctional levopimaradiene/abietadiene synthases.
2 ely resembles (46% identity, 67% similarity) abietadiene synthase, a diterpene cyclase from grand fir
3 ), along with the paralogous levopimaradiene/abietadiene synthase and isopimaradiene synthase, all of
4 nitiated cyclization was defined by modeling abietadiene synthase and locating the DXDD motif previou
5 for the cryptic insertional element found in abietadiene synthase and other diterpene synthases that
6 howed that, although the two active sites of abietadiene synthase are catalytically independent, subs
10 abolene (C(15)), delta-selinene (C(15)), and abietadiene synthase (C(20)) from Abies grandis and taxa
11 lization/rearrangement reaction catalyzed by abietadiene synthase can be similarly cut short to produ
15 --a process that requires four enzymes: one (abietadiene synthase) for conversion of the acyclic, ach
19 with the novel mechanism of the bifunctional abietadiene synthase in catalyzing both protonation-init
21 tivity of the resin acid biosynthetic enzyme abietadiene synthase is 100-fold less sensitive to [Mg(2
22 e, it was demonstrated that each reaction of abietadiene synthase is carried out at a distinct active
24 alytically distinct domains, and, therefore, abietadiene synthase is unlikely to have arisen by fusio
27 es of the isopimaradiene- or levopimaradiene/abietadiene synthase type, which employ deprotonation re
28 enzyme catalyzing the cyclization reaction, abietadiene synthase, was purified from stems of wounded
29 ses revealed an amino-terminal region of the abietadiene synthase, which resembles those of enzymes t
31 nt enzymes enhance the activity of wild-type abietadiene synthase with geranylgeranyl diphosphate as
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