abietadiene synthase

{{infobox enzyme

| Name = abieta-7,13-diene synthase

| EC_number = 4.2.3.18

| CAS_number = 157972-08-2

| GO_code = 0050554

| image =

| width =

| caption =

}}

The enzyme abieta-7,13-diene synthase (EC 4.2.3.18) catalyzes the chemical reaction

:(+)-copalyl diphosphate $\rightleftharpoons$ abieta-7,13-diene + diphosphate

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is (+)-copalyl-diphosphate diphosphate-lyase [cyclizing, abieta-7,13-diene-forming]. This enzyme is also called copalyl-diphosphate diphosphate-lyase (cyclizing). This enzyme participates in diterpenoid biosynthesis.

It has recently been shown (Keeling, et al., 2011) that the orthologous gene in Norway spruce (Picea abies) does not produce abietadiene directly, but instead produces a thermally unstable allylic tertiary alcohol 13-hydroxy-8(14)- abietene, which readily dehydrates to abietadiene, levopimaradiene, palustradiene, and neoabietadiene, when analyzed by the commonly used gas chromatography. This has been confirmed in the other conifer species, lodgepole pine (Pinus contorta) and Jack pine (Pinus banksiana) (Hall et al., 2013).

References

{{cite journal | author = RB | date = 2000 | title = Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme | journal = Biochemistry | volume = 39 | pages = 15592–602 | pmid = 11112547 | doi = 10.1021/bi001997l | last2 = Flory | first2 = JE | last3 = Jetter | first3 = R | last4 = Ravn | first4 = MM | last5 = Lee | first5 = HJ | last6 = Coates | first6 = RM | last7 = Croteau | first7 = RB | issue = 50 }}
{{cite journal |vauthors=Peters RJ, Ravn MM, Coates RM, Croteau RB | date = 2001 | title = Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites | journal = J. Am. Chem. Soc. | volume = 123 | pages = 8974–8 | pmid = 11552804 | doi = 10.1021/ja010670k | issue = 37 }}
{{cite journal |vauthors=Peters RJ, Croteau RB | date = 2002 | title = Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | pages = 580–4 | pmid = 11805316 | doi = 10.1073/pnas.022627099 | issue = 2 | pmc = 117348 | doi-access = free }}
{{cite journal |vauthors=Peters RJ, Croteau RB | date = 2002 | title = Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate | journal = Biochemistry | volume = 41 | pages = 1836–42 | pmid = 11827528 | doi = 10.1021/bi011879d | issue = 6 | url = https://works.bepress.com/reuben_peters/15/download/ | url-access = subscription }}
{{cite journal |vauthors=Ravn MM, Peters RJ, Coates RM, Croteau R | date = 2002 | title = Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates | journal = J. Am. Chem. Soc. | volume = 124 | pages = 6998–7006 | pmid = 12059223 | doi = 10.1021/ja017734b | issue = 24 }}
{{cite journal |vauthors=Keeling CI, Madilao LL, Zerbe P, Dullat HK, Bohlmann J | date = 2011 | title = The primary diterpene synthase products of Picea abies levopimaradiene/abietadiene synthase (PaLAS) are epimers of a thermally unstable diterpenol | journal = J. Biol. Chem. | volume = 286 | pages = 21145–21153 | pmid = 21518766 | doi = 10.1074/jbc.M111.245951 | issue = 24 | pmc=3122176| doi-access = free }}
{{cite journal |vauthors=Hall DE, Zerbe P, Jancsik S, Quesada AL, Dullat H, Madilao LL, Yuen M, Bohlmann J | date = 2013 | title = Evolution of conifer diterpene synthases: diterpene resin acid biosynthesis in lodgepole pine and jack pine involves monofunctional and bifunctional diterpene synthases | journal = Plant Physiol. | volume = 161 | pages = 600–616 | pmid = 23370714 | doi = 10.1104/pp.112.208546 | issue = 2 | pmc=3561007}}

Category:EC 4.2.3

Category:Enzymes of unknown structure