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farnesyl diphosphate
(E)-beta-farnesene
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-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
geranylgeranyl diphosphate
(-)-abietadiene + ?
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-
-
-
?
geranylgeranyl diphosphate
copalyl diphosphate
-
class II terpene synthase reaction
-
-
r
additional information
?
-
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
r
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
?
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
-
r
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
r
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
r
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
r
geranylgeranyl diphosphate
(+)-copalyl diphosphate
-
-
-
r
geranylgeranyl diphosphate
(+)-copalyl diphosphate
BDTC-like enzyme, miltiradiene synthase converts geranylgeranyl diphosphate to a diterpene hydrocarbon product with a molecular mass of 272 Da. Mutation in the type-B active motif of BDTC-like enzyme miltiradiene synthase, D611G/D612G, abolishes the cyclase activity, whereas (+)-copalyl diphosphate, the reaction intermediate from the conversion of geranylgeranyl diphosphate to the hydrocarbon product, rescues the cyclase activity of the mutant to form a diterpene hydrocarbon. Another mutant lacking type-A activity, D391G/D392G, accumulates copalyl diphosphate as the reaction intermediate
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?
additional information
?
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bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate to isopimara-7,15-diene
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-
?
additional information
?
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the enzyme shows substrate specificity, reaction product analysis by GC-MS. MvCPS3 does not produce ent-CPP, reaction of EC 5.5.1.13
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?
additional information
?
-
-
the enzyme shows substrate specificity, reaction product analysis by GC-MS. MvCPS3 does not produce ent-CPP, reaction of EC 5.5.1.13
-
-
?
additional information
?
-
abietadiene synthase (PaLAS) is a bifunctional terpene synthase that catalyzes both class I and class II reactions, i.e. formation of (+)-copalyl diphosphate from geranylgeranyl diphosphate (EC 5.5.1.12, class II diTPS), and formation of abieta-8(14),12-diene from (+)-copalyl diphosphate (cf. EC 4.2.3.32, class I diTPS)
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-
?
additional information
?
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the bifunctional diterpene synthase isopimara-7, 15-diene synthase (diTPS-ISO) catalyzes the cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate and the formation of isopimara-7,15-diene from (+)-copalyl diphosphate (cf. EC 4.2.3.44). Compound identification and quantification by GC-MS analysis
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-
?
additional information
?
-
gymnosperm diterpene synthases of diterpene resin acid biosynthesis are bifunctional enzymes that catalyze the initial bicyclization of geranylgeranyl diphosphate followed by rearrangement of a (+)-copalyl diphosphate intermediate at two discrete class II and class I active sites. The bifunctional jack pine and lodgepole pine LAS enzymes demonstrated that the class I active sites of monofunctional proteins can use the (+)-copalyl diphosphate intermediate produced by the class II active site of the bifunctional enzymes, overview
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?
additional information
?
-
gymnosperm diterpene synthases of diterpene resin acid biosynthesis are bifunctional enzymes that catalyze the initial bicyclization of geranylgeranyl diphosphate followed by rearrangement of a (+)-copalyl diphosphate intermediate at two discrete class II and class I active sites. The bifunctional jack pine and lodgepole pine LAS enzymes demonstrated that the class I active sites of monofunctional proteins can use the (+)-copalyl diphosphate intermediate produced by the class II active site of the bifunctional enzymes, overview
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?
additional information
?
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miltiradiene synthesis reaction with geranylgeranyl diphosphate to miltiradiene, EC 4.2.3.131, via (+)-copalyl diphosphate intermediate, not ent-copalyl diphosphate. The enzyme catalyzes the successive two-step type-B (protonation-initiated cyclization) and type-A (ionization-initiated cyclization) reactions of geranylgeranyl diphosphate. The two aspartate-rich motifs, 389DIDD and 611DDLMD, that are required for the type-B and type-A cyclization reactions, respectively. Product analysis by GC-MS and NMR spectroscopy
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?
additional information
?
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miltiradiene synthesis reaction with geranylgeranyl diphosphate to miltiradiene, EC 4.2.3.131, via (+)-copalyl diphosphate intermediate, not ent-copalyl diphosphate. The enzyme catalyzes the successive two-step type-B (protonation-initiated cyclization) and type-A (ionization-initiated cyclization) reactions of geranylgeranyl diphosphate. The two aspartate-rich motifs, 389DIDD and 611DDLMD, that are required for the type-B and type-A cyclization reactions, respectively. Product analysis by GC-MS and NMR spectroscopy
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?
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malfunction
changing two adjacent residues that seem to serve as the catalytic base in the normal CPP synthase from Salvia miltiorrhiza (SmCPS) to the residues found in the closely related perigrinol diphosphate synthase from Marrubium vulgare (MvPPS), which produces a partially rearranged and hydroxylated product derived from the distinct syn stereoisomer of labdaenyl intermediate, alters the product outcome, cf. EC 5.5.1.14. Specifically, the relevant SmCPS:H315N/T316V double mutant produces terpentedienyl diphosphate, which is derived from complete substituent rearrangement of syn rather than normal labdaenyl intermediate. Alteration of the residues that normally serve as the catalytic base can impact stereocontrol
physiological function
the chloroplastidic bifunctional diterpene synthase, isopimara-7,15-diene synthase (diTPS-ISO) from Picea abies and a cytosolic multifunctional cytochrome P450 (CYP720B4, UniProt ID E5FA70) from Picea sitchensis, which is associated to the endoplasmic reticulum. The diterpene synthase diTPS-ISO converts geranylgeranyl diphosphate (GGPP) to the tricyclic diterpene isopimara-7,15-diene (isopimaradiene)
evolution
the enzyme belongs to the class II diterpene synthases, phylogenetic tree, diterpene biosynthesis in gymnosperms, overview
evolution
the enzyme belongs to the class II diterpene synthases, phylogenetic tree, diterpene biosynthesis in gymnosperms, overview
evolution
diterpene synthases transcriptome analysis of Marrubium vulgare leaves, overview. CPS3 is a class II diterpene synthase, phylogenetic analysis
evolution
the bifunctional enzyme belongs to the class I and II diterpene synthases
evolution
the enzyme belongs to the diterpene synthase family
evolution
the enzyme is a class II diterpene cyclase
evolution
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the enzyme belongs to the diterpene synthase family
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metabolism
bifunctional class I/II PcLAS1 and PbLAS1 enzymes can supply (+)-copalyl diphosphate for the Monofunctional class I enzymes
metabolism
bifunctional diterpene cyclases are involved in hormone and defense compound biosyntheses in bryophytes and gymnosperms, respectively
metabolism
several stereoisomers of copalyl diphosphate (CDP) are found, among which the most common is ent-CDP, the precursor of gibberellins. Other isomers are syn-CDP and normal-CDP, the latter being utilized for the biosynthesis of diterpene resin acids in Gymnosperms and abietane-type tanshinones in Salvia miltiorrhiza. The second step of the cyclization is initiated through the formation of a carbocation upon ionization of the diphosphate linkage of CDP. This is catalyzed by class I terpene synthases which can transform CDP into a variety of polycyclic diterpenoids. By analogy to other labdane-type diterpenoids, the biosynthesis of the diterpene precursor of the carnosic acid pathway in rosemary proceeds in two sequential steps catalyzed by two distinct enzymes. The first is a class II TPS enzyme, CPS1, that yields normal CDP, which then is converted to miltiradiene by a KSL enzyme, miltiradiene synthase, EC 4.2.3.131, which apears in two isoforms, RoKSL1 and RoKSL2, in Rosmarinus officinalis. Hypothetical biosynthetic pathway of carnosic acid and carnosol produced in Rosmarinus officinalis, overview
metabolism
the bifunctional diterpene synthase, isopimara-7, 15-diene synthase (diTPS-ISO) and a multifunctional cytochrome P450, CYP720B4 perform the biosynthesis of isopimaric acid. The diterpene synthase converts geranylgeranyl diphosphate (GGPP) to the tricyclic diterpene isopimara-7,15-diene (isopimaradiene) via formation of (+)-copalyl diphosphate. In three subsequent oxygenation reactions, the endoplasmic reticulum-associated enzyme CYP720B4 catalyzes the conversion of isopimaradiene into isopimaric acid, pathway overview
additional information
enzyme structure by two-dimensional and three-dimensional NMR
additional information
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enzyme structure by two-dimensional and three-dimensional NMR
additional information
class II diterpene cyclases (DTCs) utilize a general acid-base catalyzed cyclo-isomerization reaction to produce various stereoisomers of the eponymous labdaenyl carbocation intermediate, which can then undergo rearrangement and/or the addition of water prior to terminating deprotonation. Identification of the pair of residues that cooperatively serves as the catalytic base in the DTCs producing ent-copalyl diphosphate (CPP) required for gibberellin phytohormone biosynthesis in all vascular plants, overview
additional information
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class II diterpene cyclases (DTCs) utilize a general acid-base catalyzed cyclo-isomerization reaction to produce various stereoisomers of the eponymous labdaenyl carbocation intermediate, which can then undergo rearrangement and/or the addition of water prior to terminating deprotonation. Identification of the pair of residues that cooperatively serves as the catalytic base in the DTCs producing ent-copalyl diphosphate (CPP) required for gibberellin phytohormone biosynthesis in all vascular plants, overview
additional information
enzyme CPS3 contains a DIDD functional motif
additional information
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enzyme CPS3 contains a DIDD functional motif
additional information
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enzyme structure homology analysis
additional information
A0A0A7AN31
metabolomic profiling, and homology modeling and molecular docking
additional information
metabolomic profiling, and homology modeling and molecular docking
additional information
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metabolomic profiling, and homology modeling and molecular docking
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D361A
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lower turnover with geranylgeranyl diphosphate than wild-type
D402A
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lower turnover with geranylgeranyl diphosphate than wild-type
D402E
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lower turnover with geranylgeranyl diphosphate than wild-type
D402N
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lower turnover with geranylgeranyl diphosphate than wild-type
D404E
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lower turnover with geranylgeranyl diphosphate than wild-type
D404N
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lower turnover with geranylgeranyl diphosphate than wild-type
D405A
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lower turnover with geranylgeranyl diphosphate than wild-type
D405E
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lower turnover with geranylgeranyl diphosphate than wild-type
D405N
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lower turnover with geranylgeranyl diphosphate than wild-type
D625A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
D766A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
D845A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
DELTA:107-868
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lower turnover with copalyl diphosphate than wild-type
DELTA:85-849
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no turnover with copalyl diphosphate
E499A
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lower turnover with geranylgeranyl diphosphate than wild-type
E589A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
E699A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
E773A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
E778A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
N765A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
R365A
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lower turnover with geranylgeranyl diphosphate than wild-type
R411A
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lower turnover with geranylgeranyl diphosphate than wild-type
R454A
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lower turnover with geranylgeranyl diphosphate than wild-type
R584A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
R586A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
R762A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
rAS:D96A
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nearly the same turnover with copalyl diphosphate like wild-type
rAS:K86A/R87A
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lower turnover with copalyl diphosphate than wild-type
S721A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
T617A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
T848A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
W358A
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lower turnover with geranylgeranyl diphosphate than wild-type
Y520A
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lower turnover with geranylgeranyl diphosphate than wild-type
Y841F
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
H315N/T316V
site-directed mutagenesis, the double mutant produces terpentedienyl diphosphate, which is derived from complete substituent rearrangement of syn rather than normal labdaenyl intermediate. Alteration of the residues that normally serve as the catalytic base can impact stereocontrol
D391G/D392G
site-directed mutagenesis of DIDD motif residues, the mutant lacks type-B activity
D611G/D612G
site-directed mutagenesis of DDLMD motif residues, the mutant lacks type-A cyclase activity
D404A
-
-
D404A
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unreactive with geranylgeranyl diphosphate
D621A
-
-
D621A
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unreactive with (+)-copalyl diphosphate
D621A
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eliminates class I activity
T769A
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no effect on geranylgeranyl diphosphate reaction, but lower turnover with copalyl diphosphate than wild-type
additional information
transient heterologous expression of the isopimaric acid pathway in Nicotiana benthamiana. Expressing DXS and GGPPs from Plectranthus barbatus in Nicotiana benthamiana are efficient in boosting diterpenoid levels compared to coexpression of the Nicotiana endogenous DXS and GGPPs genes, which have no effect on boosting diterpenoid level. Pigment analysis of infiltrated leaves, overview
additional information
using a combination of protein and genetic engineering, significant improvements in the production of sclareol and several other isoprenoids is achieved, including cis-abienol, abietadiene, and beta-carotene. Recombinant expression of enzyme PaLAS in Saccharomyces cerevisiae AM94 cells, coexpression with different Saccharomyces cerevisiae farnesyl diphosphate synthase ERG20 variants increases diterpene yields by up to 15fold compared to expression of the Cistus creticus GGPPS
additional information
A0A0A7AN31
knockdown of SmCPS1 by RNAi
additional information
knockdown of SmCPS1 by RNAi
additional information
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knockdown of SmCPS1 by RNAi
-
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DNA and amino acid sequence determination and analysis of 18 different amino acid sequence of copalyl diphosphate synthase, CPS, phylogenetic analysis and tree
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expression in Escherichia coli
expression of His-tagged enzyme in Escherichia coli
functional expression of Picea abies isopimara-7,15-diene synthase (diTPS-ISO) in Nicotiana benthamiana leaves via Agrobacterium tumefaciens transfection method, coexpression with a multifunctional cytochrome P450 (CYP720B4) from Picea sitchensis, subcloning in Escherichia coli strain NEB10beta
gene CPS1, phylogenetic analysis and tree, functional recombinant expression in Saccharomyces cerevisiae strain AM113, with co-overexpressing of GGDPS1 from Cistus creticus, and Nicotiana benthamiana, heterologous expression of the RoCPS1 protein in Escherichia coli fails
gene CPS3, phylogenetic analysis and tree, quantitative expression analysis, functional expression of MvCPS3 alone or with MvELS (multifunctional betaalpha-domain class I diterpene synthase) or MvEKS (ent-kaurene synthase) in engineered Nicotiana benthamiana
gene SmCPS1, phylogenetic analysis, a 289-bp gene-specific sequence including the 3' UTR of SmCPS1 is amplified by PCR using cDNA as a template and then cloned into the pK7GWIWG (II) binary, then introduced into Agrobacterium tumefaciens strain EHA105 by electroporation for ransformation of leaf explants from Salvia miltiorrhiza bh2-7 plants, recombinant expression of His-tagged enzyme in Escherichia coli strains Tuner (DE3) or Origami B (DE3)
gene SmCPS2, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strains Tuner (DE3) or Origami B (DE3)
gene TPS-LAS, recombinant expression in Saccharomyces cerevisiae strain AM94, a yeast strain engineered for the production of isoprenoids, which contains three chromosomally integrated copies of a degradation stabilized variant of HMG2 and a heterozygous deletion of ERG9, and in strain AM204, each with or without coexpression of yeast protein Erg20p(F96C), a yeast FPP synthase, overview
Site-directed mutagenesis is carried out via PCR amplification with overlapping mutagenic primers, and the mutant genes verify by complete sequencing. The resulting wild type and mutant genes are then transferred via directional recombination to the T7-promoter and N-terminal 6xhis fusion expression vector pDEST17. Use of the pDEST17 vector results in a 25 amino acid residue linker between the 6 His-tag and the cloned protein.
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expression in Escherichia coli
-
expression in Escherichia coli
-
expression of His-tagged enzyme in Escherichia coli
expression of His-tagged enzyme in Escherichia coli
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LeFever, R.E.; Vogel, B.S.; Croteau, R.
Diterpenoid resin acid biosynthesis in conifers: enzymic cyclization of geranylgeranyl pyrophosphate to abietadiene, the precursor of abietic acid
Arch. Biochem. Biophys.
313
139-149
1994
Abies grandis, Pinus contorta
brenda
Ravn, M.M.; Coates, R.M.; Jetter, R.; Croteau, R.B.
Stereospecific intramolecular proton transfer in the cyclization of geranylgeranyl diphosphate to (-)-abietadiene catalyzed by recombinant cyclase from grand fir (Abies grandis)
Chem. Commun. (Camb.)
1998
21-22
1998
Abies grandis, Pinus contorta
-
brenda
Ravn, M.M.; Coates, R.M.; Flory, J.E.; Peters, R.J.; Croteau, R.
Stereochemistry of the cyclization-rearrangement of (+)-copalyl diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene synthase from Abies grandis
Org. Lett.
2
573-576
2000
Abies grandis
brenda
Peters, R.J.; Flory, J.E.; Jetter, R.; Ravn, M.M.; Lee, H.J.; Coates, R.M.; Croteau, R.B.
Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme
Biochemistry
39
15592-15602
2000
Abies grandis
brenda
Peters, R.J.; Ravn, M.M.; Coates, R.M.; Croteau, R.B.
Bifunctional abietadiene synthase: Free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites
J. Am. Chem. Soc.
123
8974-8978
2001
Abies grandis
brenda
Peters, R.J.; Croteau, R.B.
Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate
Biochemistry
41
1836-1842
2002
Abies grandis
brenda
Peters, R.J.; Croteau, R.B.
Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement
Proc. Natl. Acad. Sci. USA
99
580-584
2002
Abies grandis
brenda
Ravn, M.M.; Peters, R.J.; Coates, R.M.; Croteau, R.
Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates
J. Am. Chem. Soc.
124
6998-7006
2002
Abies grandis
brenda
Peters, R.J.; Carter, O.A.; Zhang, Y.; Matthews, B.W.; Croteau, R.B.
Bifunctional abietadiene synthase: mutual structural dependence of the active sites for protonation-initiated and ionization-initiated cyclizations
Biochemistry
42
2700-2707
2003
Abies grandis
brenda
Smith, M.W.; Yamaguchi, S.; Ait-Ali, T.; Kamiya, Y.
The first step of gibberellin biosynthesis in pumpkin is catalyzed by at least two copalyl diphosphate synthases encoded by differentially regulated genes
Plant Physiol.
118
1411-1419
1998
Cucurbita maxima
brenda
Tudzynski, B.; Kawaide, H.; Kamiya, Y.
Gibberellin biosynthesis in Gibberella fujikuroi: cloning and characterization of the copalyl diphosphate synthase gene
Curr. Genet.
34
234-240
1998
Fusarium fujikuroi
brenda
Zhou, K.; Peters, R.J.
Investigating the conservation pattern of a putative second terpene synthase divalent metal binding motif in plants
Phytochemistry
70
366-369
2009
Abies grandis
brenda
Sugai, Y.; Ueno, Y.; Hayashi, K.; Oogami, S.; Toyomasu, T.; Matsumoto, S.; Natsume, M.; Nozaki, H.; Kawaide, H.
Enzymatic (13)C labeling and multidimensional NMR analysis of miltiradiene synthesized by bifunctional diterpene cyclase in Selaginella moellendorffii
J. Biol. Chem.
286
42840-42847
2011
Selaginella moellendorffii (G9MAN7), Selaginella moellendorffii
brenda
Zerbe, P.; Chiang, A.; Yuen, M.; Hamberger, B.; Hamberger, B.; Draper, J.A.; Britton, R.; Bohlmann, J.
Bifunctional cis-abienol synthase from Abies balsamea discovered by transcriptome sequencing and its implications for diterpenoid fragrance production
J. Biol. Chem.
287
12121-12131
2012
Abies balsamea (H8ZM71)
brenda
Hall, D.; Zerbe, P.; Jancsik, S.; Quesada, A.; Dullat, H.; Madilao, L.; Yuen, M.; Bohlmann, J.
Evolution of conifer diterpene synthases: diterpene resin acid biosynthesis in lodgepole pine and jack pine involves monofunctional and bifunctional diterpene synthases
Plant Physiol.
161
600-616
2013
Pinus banksiana (M4HXU6), Pinus contorta (M4HXW7)
brenda
Brueckner, K.; Bozic, D.; Manzano, D.; Papaefthimiou, D.; Pateraki, I.; Scheler, U.; Ferrer, A.; de Vos, R.C.; Kanellis, A.K.; Tissier, A.
Characterization of two genes for the biosynthesis of abietane-type diterpenes in rosemary (Rosmarinus officinalis) glandular trichomes
Phytochemistry
101
52-64
2014
Salvia rosmarinus (W8QQT6), Salvia rosmarinus
brenda
Zerbe, P.; Chiang, A.; Dullat, H.; ONeil-Johnson, M.; Starks, C.; Hamberger, B.; Bohlmann, J.
Diterpene synthases of the biosynthetic system of medicinally active diterpenoids in Marrubium vulgare
Plant J.
79
914-927
2014
Marrubium vulgare (A0A075FA51), Marrubium vulgare
brenda
Cui, G.; Duan, L.; Jin, B.; Qian, J.; Xue, Z.; Shen, G.; Snyder, J.H.; Song, J.; Chen, S.; Huang, L.; Peters, R.J.; Qi, X.
Functional divergence of diterpene syntheses in the medicinal plant Salvia miltiorrhiza
Plant Physiol.
169
1607-1618
2015
Salvia miltiorrhiza f. alba (A0A0A7AN31), Salvia miltiorrhiza f. alba (A0A0A7ANT1), Salvia miltiorrhiza f. alba bh2-7 (A0A0A7AN31), Salvia miltiorrhiza f. alba bh2-7 (A0A0A7ANT1)
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Schulte, S.; Potter, K.C.; Lemke, C.; Peters, R.J.
Catalytic bases and stereocontrol in Lamiaceae class II diterpene cyclases
Biochemistry
57
3473-3479
2018
Salvia miltiorrhiza (B8PQ84), Salvia miltiorrhiza
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Li, Q.; Di, P.; Lu, W.; Zhang, L.; Chen, W.
Bioinformatics analysis of copalyl diphosphate synthase in Salviae Miltiorrhizae Radix et Rhizoma
Chin. Tradit. Herbal Drugs
46
887-894
2015
Salvia miltiorrhiza
-
brenda
Gnanasekaran, T.; Vavitsas, K.; Andersen-Ranberg, J.; Nielsen, A.Z.; Olsen, C.E.; Hamberger, B.; Jensen, P.E.
Heterologous expression of the isopimaric acid pathway in Nicotiana benthamiana and the effect of N-terminal modifications of the involved cytochrome P450 enzyme
J. Biol. Eng.
9
24
2015
Picea abies (Q675L5)
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Ignea, C.; Trikka, F.; Nikolaidis, A.; Georgantea, P.; Ioannou, E.; Loupassaki, S.; Kefalas, P.; Kanellis, A.; Roussis, V.; Makris, A.; Kampranis, S.
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Metab. Eng.
27
65-75
2015
Picea abies (Q675L4)
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