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Literature summary for 4.2.3.19 extracted from

  • Jia, M.; Peters, R.J.
    Extending a single residue switch for abbreviating catalysis in plant ent-kaurene synthases (2016), Front. Plant Sci., 7, 1765 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.3.19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli OverExpress C41 cells Physcomitrium patens
expressed in Escherichia coli OverExpress C41 cells Arabidopsis thaliana
expressed in Escherichia coli OverExpress C41 cells Selaginella moellendorffii
expressed in Escherichia coli OverExpress C41 cells Oryza sativa Japonica Group
expressed in Escherichia coli OverExpress C41 cells Picea glauca
expressed in Escherichia coli OverExpress C41 cells Marchantia polymorpha subsp. ruderalis
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3) Physcomitrium patens
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3) Arabidopsis thaliana
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3) Oryza sativa Japonica Group
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3) Picea glauca
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3) Marchantia polymorpha subsp. ruderalis
sequence comparisons, recombinant expression of wild-type enzyme in Escherichia coli strain C41(DE3) Selaginella moellendorffii

Protein Variants

Protein Variants Comment Organism
I368A the mutant produces ent-pimara-8(14),15-diene, ent-kaur-16-ene, 8alpha-hydroxy-ent-pimara-15-ene, and ent-pimara-7,15-diene from ent-copalyl diphosphate Arabidopsis thaliana
I368S the mutant produces ent-pimara-8(14),15-diene and 8alpha-hydroxy-ent-pimara-15-ene from ent-copalyl diphosphate Arabidopsis thaliana
I368T the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate Arabidopsis thaliana
I368V the mutant produces ent-kaur-16-ene from ent-copalyl diphosphate Arabidopsis thaliana
I619A site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme Picea glauca
I638A site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces a mixture of four products, pedominantly ent-pimara-8(14),15-diene, and a small amount of the double bond isomer ent-pimara-7,15-diene, and variable amounts of ent-kaur-16-ene, as well as substantial amounts of 8a-hydroxy-ent-pimar-15-ene Arabidopsis thaliana
I638S site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces a mixture of four products, pedominantly ent-pimara-8(14),15-diene, and a small amount of the double bond isomer ent-pimara-7,15-diene, and variable amounts of ent-kaur-16-ene, as well as substantial amounts of 8a-hydroxy-ent-pimar-15-ene Arabidopsis thaliana
I638T site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces a mixture of four products, pedominantly ent-pimara-8(14),15-diene, and small amounts of the double bond isomer ent-pimara-7,15-diene and 8a-hydroxy-ent-pimar-15-ene, and variable amounts of ent-kaur-16-ene Arabidopsis thaliana
I638V site-directed mutagenesis, the mutant shows unaltered product spectrum compared to the wild-type enzyme and produces just ent-kaur-16-ene Arabidopsis thaliana
I645T site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces almost entirely ent-pimara-8(14),15-diene, reaction of EC 4.2.3.30 Marchantia polymorpha subsp. ruderalis
I645T the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate Marchantia polymorpha subsp. ruderalis
I664A site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces significant amounts of 8alpha-hydroxy-ent-pimara-15-ene generated by addition of water prior to deprotonation, it also produces ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate Oryza sativa Japonica Group
I664S site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces significant amounts of 8alpha-hydroxy-ent-pimara-15-ene generated by addition of water prior to deprotonation, it also produces ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate Oryza sativa Japonica Group
I664T site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces high amounts of ent-pimara-8(14),15-diene, it also produces ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate Oryza sativa Japonica Group
I664V site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces ent-isokaurene and ent-copalol, the dephosphorylated derivative of ent-copalyl diphosphate Oryza sativa Japonica Group
I741T site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme, the mutant produces almost entirely ent-pimara-8(14),15-diene, reaction of EC 4.2.3.30 Physcomitrium patens
I741T the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate Physcomitrium patens

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Physcomitrium patens 9507
-
chloroplast
-
 Arabidopsis thaliana 9507
-
chloroplast
-
 Selaginella moellendorffii 9507
-
chloroplast
-
 Oryza sativa Japonica Group 9507
-
chloroplast
-
 Picea glauca 9507
-
chloroplast
-
 Marchantia polymorpha subsp. ruderalis 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ent-copalyl diphosphate Physcomitrium patens
-
 ent-kaur-16-ene + 6alpha-hydroxy-ent-kaurane + diphosphate
-
 ?
ent-copalyl diphosphate Physcomitrium patens
-
 ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate Arabidopsis thaliana
-
 ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate Selaginella moellendorffii
-
 ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate Oryza sativa Japonica Group
-
 ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate Picea glauca
-
 ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate Marchantia polymorpha subsp. ruderalis
-
 ent-kaur-16-ene + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9SAK2
-
-
Marchantia polymorpha subsp. ruderalis A0A176VPW0
-
-
Oryza sativa Japonica Group Q0JA82
-
-
Physcomitrium patens A5A8G0
-
-
Picea glauca D2XEB3
-
-
Selaginella moellendorffii A0A077JGG8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3) Physcomitrium patens
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3) Arabidopsis thaliana
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3) Oryza sativa Japonica Group
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3) Picea glauca
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3) Marchantia polymorpha subsp. ruderalis
recombinant wild-type enzyme from Escherichia coli strain C41(DE3) Selaginella moellendorffii

Reaction

Reaction Comment Organism Reaction ID
ent-copalyl diphosphate = ent-kaurene + diphosphate cyclization mechanism catalyzed by KSs and the Ile mutants, via ent-pimar-15-en-8-yl, ent-beyeran-16-yl, and ent-kauran-16-yl intermediates, detailed overview Physcomitrium patens
a
ent-copalyl diphosphate = ent-kaurene + diphosphate cyclization mechanism catalyzed by KSs and the Ile mutants, via ent-pimar-15-en-8-yl, ent-beyeran-16-yl, and ent-kauran-16-yl intermediates, detailed overview Arabidopsis thaliana
a
ent-copalyl diphosphate = ent-kaurene + diphosphate cyclization mechanism catalyzed by KSs and the Ile mutants, via ent-pimar-15-en-8-yl, ent-beyeran-16-yl, and ent-kauran-16-yl intermediates, detailed overview Selaginella moellendorffii
a
ent-copalyl diphosphate = ent-kaurene + diphosphate cyclization mechanism catalyzed by KSs and the Ile mutants, via ent-pimar-15-en-8-yl, ent-beyeran-16-yl, and ent-kauran-16-yl intermediates, detailed overview Oryza sativa Japonica Group
a
ent-copalyl diphosphate = ent-kaurene + diphosphate cyclization mechanism catalyzed by KSs and the Ile mutants, via ent-pimar-15-en-8-yl, ent-beyeran-16-yl, and ent-kauran-16-yl intermediates, detailed overview Picea glauca
a
ent-copalyl diphosphate = ent-kaurene + diphosphate cyclization mechanism catalyzed by KSs and the Ile mutants, via ent-pimar-15-en-8-yl, ent-beyeran-16-yl, and ent-kauran-16-yl intermediates, detailed overview Marchantia polymorpha subsp. ruderalis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ent-copalyl diphosphate enzyme OsKSL5i, via the ent-kauran-16-yl intermediate, overview Oryza sativa Japonica Group ent-isokaur-15-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Physcomitrium patens ent-kaur-16-ene + 6alpha-hydroxy-ent-kaurane + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Physcomitrium patens ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Arabidopsis thaliana ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Selaginella moellendorffii ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Oryza sativa Japonica Group ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Picea glauca ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate
-
 Marchantia polymorpha subsp. ruderalis ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate almost exclusive production of ent-kaurene and 16alpha-hydroxy-ent-kaur-ene by the wild-type PpCPS/KS enzyme, while mutant I741T shows ent-pimara-8(14),15-diene synthase activity, EC 4.2.3.30 Physcomitrium patens ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate almost exclusive production of ent-kaurene by the wild-type MpKS enzyme, while mutant I645T shows ent-pimara-8(14),15-diene synthase activity, EC 4.2.3.30 Marchantia polymorpha subsp. ruderalis ent-kaur-16-ene + diphosphate
-
 ?
ent-copalyl diphosphate + H2O almost exclusive production of ent-kaurene and 16alpha-hydroxy-ent-kaur-ene by the wild-type PpCPS/KS enzyme, while mutant I741T shows ent-pimara-8(14),15-diene synthase activity, EC 4.2.3.30 Physcomitrium patens 16alpha-hydroxy-ent-kaur-ene + diphosphate
-
 ?
additional information GC-MS analysis of products, overview Physcomitrium patens ?
-
 ?
additional information GC-MS analysis of products, overview Arabidopsis thaliana ?
-
 ?
additional information GC-MS analysis of products, overview Selaginella moellendorffii ?
-
 ?
additional information GC-MS analysis of products, overview Oryza sativa Japonica Group ?
-
 ?
additional information GC-MS analysis of products, overview Picea glauca ?
-
 ?
additional information GC-MS analysis of products, overview Marchantia polymorpha subsp. ruderalis ?
-
 ?

Synonyms

Synonyms Comment Organism
(-)-ent-kaurene synthase
-
 Picea glauca
AtKS
-
 Arabidopsis thaliana
bifunctional CPS/KS
-
 Physcomitrium patens
bifunctional CPS/KS
-
 Selaginella moellendorffii
ent-kaur-16-ene synthase
-
 Arabidopsis thaliana
ent-kaur-16-ene synthase
-
 Oryza sativa Japonica Group
KS1A UniProt Oryza sativa Japonica Group
KSL5
-
 Oryza sativa Japonica Group
MpKS
-
 Marchantia polymorpha subsp. ruderalis
PgKS
-
 Picea glauca
PpCPS/KS
-
 Physcomitrium patens
SmKS
-
 Selaginella moellendorffii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Physcomitrium patens
37
-
 assay at Arabidopsis thaliana
37
-
 assay at Selaginella moellendorffii
37
-
 assay at Oryza sativa Japonica Group
37
-
 assay at Picea glauca
37
-
 assay at Marchantia polymorpha subsp. ruderalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Physcomitrium patens
7
-
 assay at Arabidopsis thaliana
7
-
 assay at Selaginella moellendorffii
7
-
 assay at Oryza sativa Japonica Group
7
-
 assay at Picea glauca
7
-
 assay at Marchantia polymorpha subsp. ruderalis

General Information

General Information Comment Organism
evolution production of ent-kaurene as a precursor for important signaling molecules such as the gibberellins seems to have arisen early in plant evolution, with corresponding cyclase(s) present in all land plants (i.e., embryophyta). The relevant enzymes seem to represent fusion of the class II diterpene cyclase that produces the intermediate ent-copalyl diphosphate (ent-CPP) and the subsequently acting class I diterpene synthase that produces ent-kaurene, although the bifunctionality of the ancestral gene is only retained in certain early diverging plants, with gene duplication and sub-functionalization leading to distinct ent-CPP synthases and ent-kaurene synthases (KSs) generally observed Physcomitrium patens
evolution production of ent-kaurene as a precursor for important signaling molecules such as the gibberellins seems to have arisen early in plant evolution, with corresponding cyclase(s) present in all land plants (i.e., embryophyta). The relevant enzymes seem to represent fusion of the class II diterpene cyclase that produces the intermediate ent-copalyl diphosphate (ent-CPP) and the subsequently acting class I diterpene synthase that produces ent-kaurene, although the bifunctionality of the ancestral gene is only retained in certain early diverging plants, with gene duplication and sub-functionalization leading to distinct ent-CPP synthases and ent-kaurene synthases (KSs) generally observed Arabidopsis thaliana
evolution production of ent-kaurene as a precursor for important signaling molecules such as the gibberellins seems to have arisen early in plant evolution, with corresponding cyclase(s) present in all land plants (i.e., embryophyta). The relevant enzymes seem to represent fusion of the class II diterpene cyclase that produces the intermediate ent-copalyl diphosphate (ent-CPP) and the subsequently acting class I diterpene synthase that produces ent-kaurene, although the bifunctionality of the ancestral gene is only retained in certain early diverging plants, with gene duplication and sub-functionalization leading to distinct ent-CPP synthases and ent-kaurene synthases (KSs) generally observed Selaginella moellendorffii
evolution production of ent-kaurene as a precursor for important signaling molecules such as the gibberellins seems to have arisen early in plant evolution, with corresponding cyclase(s) present in all land plants (i.e., embryophyta). The relevant enzymes seem to represent fusion of the class II diterpene cyclase that produces the intermediate ent-copalyl diphosphate (ent-CPP) and the subsequently acting class I diterpene synthase that produces ent-kaurene, although the bifunctionality of the ancestral gene is only retained in certain early diverging plants, with gene duplication and sub-functionalization leading to distinct ent-CPP synthases and ent-kaurene synthases (KSs) generally observed Oryza sativa Japonica Group
evolution production of ent-kaurene as a precursor for important signaling molecules such as the gibberellins seems to have arisen early in plant evolution, with corresponding cyclase(s) present in all land plants (i.e., embryophyta). The relevant enzymes seem to represent fusion of the class II diterpene cyclase that produces the intermediate ent-copalyl diphosphate (ent-CPP) and the subsequently acting class I diterpene synthase that produces ent-kaurene, although the bifunctionality of the ancestral gene is only retained in certain early diverging plants, with gene duplication and sub-functionalization leading to distinct ent-CPP synthases and ent-kaurene synthases (KSs) generally observed Picea glauca
evolution production of ent-kaurene as a precursor for important signaling molecules such as the gibberellins seems to have arisen early in plant evolution, with corresponding cyclase(s) present in all land plants (i.e., embryophyta). The relevant enzymes seem to represent fusion of the class II diterpene cyclase that produces the intermediate ent-copalyl diphosphate (ent-CPP) and the subsequently acting class I diterpene synthase that produces ent-kaurene, although the bifunctionality of the ancestral gene is only retained in certain early diverging plants, with gene duplication and sub-functionalization leading to distinct ent-CPP synthases and ent-kaurene synthases (KSs) generally observed Marchantia polymorpha subsp. ruderalis
malfunction substitution of threonine for a conserved isoleucine has been shown to short-circuit the complex bicyclization and rearrangement reaction catalyzed by ent-kaurene synthases (KSs) after initial cyclization, leading to predominant production of ent-pimaradiene, at least in KSs from angiosperms. This effect extends to KSs from earlier diverging plants (i.e., bryophytes), including a bifunctional/KS. A dramatic effect of this single residue switch on product outcome to electrostatic stabilization of the ent-pimarenyl carbocation intermediate formed upon initial cyclization by the hydroxyl introduced by threonine substitution is paralleled by similar effects from substitution of alanine Physcomitrium patens
malfunction substitution of threonine for a conserved isoleucine has been shown to short-circuit the complex bicyclization and rearrangement reaction catalyzed by ent-kaurene synthases (KSs) after initial cyclization, leading to predominant production of ent-pimaradiene, at least in KSs from angiosperms. This effect extends to KSs from earlier diverging plants (i.e., bryophytes), including a bifunctional/KS. A dramatic effect of this single residue switch on product outcome to electrostatic stabilization of the ent-pimarenyl carbocation intermediate formed upon initial cyclization by the hydroxyl introduced by threonine substitution is paralleled by similar effects from substitution of alanine Arabidopsis thaliana
malfunction substitution of threonine for a conserved isoleucine has been shown to short-circuit the complex bicyclization and rearrangement reaction catalyzed by ent-kaurene synthases (KSs) after initial cyclization, leading to predominant production of ent-pimaradiene, at least in KSs from angiosperms. This effect extends to KSs from earlier diverging plants (i.e., bryophytes), including a bifunctional/KS. A dramatic effect of this single residue switch on product outcome to electrostatic stabilization of the ent-pimarenyl carbocation intermediate formed upon initial cyclization by the hydroxyl introduced by threonine substitution is paralleled by similar effects from substitution of alanine Selaginella moellendorffii
malfunction substitution of threonine for a conserved isoleucine has been shown to short-circuit the complex bicyclization and rearrangement reaction catalyzed by ent-kaurene synthases (KSs) after initial cyclization, leading to predominant production of ent-pimaradiene, at least in KSs from angiosperms. This effect extends to KSs from earlier diverging plants (i.e., bryophytes), including a bifunctional/KS. A dramatic effect of this single residue switch on product outcome to electrostatic stabilization of the ent-pimarenyl carbocation intermediate formed upon initial cyclization by the hydroxyl introduced by threonine substitution is paralleled by similar effects from substitution of alanine Oryza sativa Japonica Group
malfunction substitution of threonine for a conserved isoleucine has been shown to short-circuit the complex bicyclization and rearrangement reaction catalyzed by ent-kaurene synthases (KSs) after initial cyclization, leading to predominant production of ent-pimaradiene, at least in KSs from angiosperms. This effect extends to KSs from earlier diverging plants (i.e., bryophytes), including a bifunctional/KS. A dramatic effect of this single residue switch on product outcome to electrostatic stabilization of the ent-pimarenyl carbocation intermediate formed upon initial cyclization by the hydroxyl introduced by threonine substitution is paralleled by similar effects from substitution of alanine Picea glauca
malfunction substitution of threonine for a conserved isoleucine has been shown to short-circuit the complex bicyclization and rearrangement reaction catalyzed by ent-kaurene synthases (KSs) after initial cyclization, leading to predominant production of ent-pimaradiene, at least in KSs from angiosperms. This effect extends to KSs from earlier diverging plants (i.e., bryophytes), including a bifunctional/KS. A dramatic effect of this single residue switch on product outcome to electrostatic stabilization of the ent-pimarenyl carbocation intermediate formed upon initial cyclization by the hydroxyl introduced by threonine substitution is paralleled by similar effects from substitution of alanine Marchantia polymorpha subsp. ruderalis
metabolism the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones. Production of ent-kaur-16-ene from the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) proceeds via two distinct bicyclization reactions. The first is catalyzed by copalyl diphosphate synthases (CPSs, EC 5.5.1.13) that are representative of class II diterpene cyclases and produce ent-copalyl diphosphate. This is then subsequently further cyclized and rearranged by ent-kaurene synthases (KSs) Physcomitrium patens
metabolism the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones. Production of ent-kaur-16-ene from the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) proceeds via two distinct bicyclization reactions. The first is catalyzed by copalyl diphosphate synthases (CPSs, EC 5.5.1.13) that are representative of class II diterpene cyclases and produce ent-copalyl diphosphate. This is then subsequently further cyclized and rearranged by ent-kaurene synthases (KSs) Arabidopsis thaliana
metabolism the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones. Production of ent-kaur-16-ene from the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) proceeds via two distinct bicyclization reactions. The first is catalyzed by copalyl diphosphate synthases (CPSs, EC 5.5.1.13) that are representative of class II diterpene cyclases and produce ent-copalyl diphosphate. This is then subsequently further cyclized and rearranged by ent-kaurene synthases (KSs) Selaginella moellendorffii
metabolism the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones. Production of ent-kaur-16-ene from the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) proceeds via two distinct bicyclization reactions. The first is catalyzed by copalyl diphosphate synthases (CPSs, EC 5.5.1.13) that are representative of class II diterpene cyclases and produce ent-copalyl diphosphate. This is then subsequently further cyclized and rearranged by ent-kaurene synthases (KSs) Oryza sativa Japonica Group
metabolism the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones. Production of ent-kaur-16-ene from the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) proceeds via two distinct bicyclization reactions. The first is catalyzed by copalyl diphosphate synthases (CPSs, EC 5.5.1.13) that are representative of class II diterpene cyclases and produce ent-copalyl diphosphate. This is then subsequently further cyclized and rearranged by ent-kaurene synthases (KSs) Picea glauca
metabolism the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones. Production of ent-kaur-16-ene from the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) proceeds via two distinct bicyclization reactions. The first is catalyzed by copalyl diphosphate synthases (CPSs, EC 5.5.1.13) that are representative of class II diterpene cyclases and produce ent-copalyl diphosphate. This is then subsequently further cyclized and rearranged by ent-kaurene synthases (KSs) Marchantia polymorpha subsp. ruderalis
additional information the hydroxyl group of the Thr638 side chain enables occasional addition of water Arabidopsis thaliana
additional information the hydroxyl group of the Thr664 side chain enables occasional addition of water Oryza sativa Japonica Group
physiological function the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones Physcomitrium patens
physiological function the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones Arabidopsis thaliana
physiological function the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones Selaginella moellendorffii
physiological function the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones Oryza sativa Japonica Group
physiological function the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones Picea glauca
physiological function the enzyme produces the diterpene ent-kaur-16-ene, which in vascular plants (i.e., tracheophytes) serves as an intermediate in biosynthesis of the gibberellin phytohormones Marchantia polymorpha subsp. ruderalis