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1 cyclization of geranylgeranyl diphosphate to abietadiene.
2 eranyl diphosphate (8, GGPP) to a mixture of abietadiene (1a), double bond isomers 2a-4a and pimaradi
3 eranyl diphosphate to the polycyclic, chiral abietadiene (a complex process involving the copalyl dip
4 ent of pine resin, is naturally derived from abietadiene --a process that requires four enzymes: one
5 stic implications for enzymatic catalysis of abietadiene cyclization, and terpene synthases more broa
6 n reactions in the formation of a mixture of abietadiene double bond isomers as the committed step in
7 f geranylgeranyl diphosphate to a mixture of abietadiene double bond isomers as the initial step of r
8 esin acid biosynthesis, forming a mixture of abietadiene double-bond isomers by two sequential, mecha
9 ulations of the key step in the formation of abietadiene (in the gas phase and in the absence of the
10 iphosphate, in the formation of a mixture of abietadiene isomers as the committed step of diterpenoid
11 l abietenyl carbocation provide a mixture of abietadiene, levopimaradiene, and neoabietadiene, and th
12 lyl diphosphate to a nearly equal mixture of abietadiene, levopimaradiene, and neoabietadiene, as wel
13 synthase must intervene in order to produce abietadiene selectively, in essence steering this reacti
16 abolene (C(15)), delta-selinene (C(15)), and abietadiene synthase (C(20)) from Abies grandis and taxa
17 ), along with the paralogous levopimaradiene/abietadiene synthase and isopimaradiene synthase, all of
18 nitiated cyclization was defined by modeling abietadiene synthase and locating the DXDD motif previou
19 for the cryptic insertional element found in abietadiene synthase and other diterpene synthases that
20 howed that, although the two active sites of abietadiene synthase are catalytically independent, subs
22 lization/rearrangement reaction catalyzed by abietadiene synthase can be similarly cut short to produ
29 with the novel mechanism of the bifunctional abietadiene synthase in catalyzing both protonation-init
31 tivity of the resin acid biosynthetic enzyme abietadiene synthase is 100-fold less sensitive to [Mg(2
32 e, it was demonstrated that each reaction of abietadiene synthase is carried out at a distinct active
34 alytically distinct domains, and, therefore, abietadiene synthase is unlikely to have arisen by fusio
37 es of the isopimaradiene- or levopimaradiene/abietadiene synthase type, which employ deprotonation re
39 nt enzymes enhance the activity of wild-type abietadiene synthase with geranylgeranyl diphosphate as
40 --a process that requires four enzymes: one (abietadiene synthase) for conversion of the acyclic, ach
41 ely resembles (46% identity, 67% similarity) abietadiene synthase, a diterpene cyclase from grand fir
42 enzyme catalyzing the cyclization reaction, abietadiene synthase, was purified from stems of wounded
43 ses revealed an amino-terminal region of the abietadiene synthase, which resembles those of enzymes t
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