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Information on EC 4.2.3.19 - ent-kaurene synthase
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EC Tree
4.2.3.19 ent-kaurene synthaseIUBMB Comments
Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase)
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Word Map
- 4.2.3.19
- gibberellin
-
diterpene
-
geranylgeranyl
-
diterpenoids
-
ent-kaurenoic
- fujikuroi
-
labdane-related
-
ditpss
- steviol
- ga20ox
-
3-oxidase
- phaeosphaeria
- ent-cps
-
ks-like
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ent-kaurene synthase, ppcps/ks, kaurene synthase, cps/ks, ent-kaurene synthase b, ent-ks, ent-copalyl/ent-kaurene synthase, bifunctional cps/ks, ent-kaur-16-ene synthase, ent-copalyldiphosphate synthase/ent-kaurene synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional CPS/KS
BjKS
blr2150
copalyl diphosphate/kaurene synthase
CPS/KS
ent-copalyl/ent-kaurene synthase
ent-kaur-16-ene synthase
ent-kaurene synthase
ent-kaurene synthase B
ent-kaurene synthetase B
-
-
-
-
ent-KS
FfCPS/KS
KS
PpCPS/KS
SmKS
additional information
CPS/KS
-
bifunctional enzyme with terpene synthase and ent-kaurene synthase activities
ent-kaur-16-ene synthase
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
-
ent-kaurene synthase B
-
-
-
-
PpCPS/KS
bifunctional cyclase with copalyl disphosphatase and kaurene synthase activity
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
-
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
additional information
-
part of bifunctional enzyme catalyzing the two step reaction from trans-geranylgeranyl-diphosphate to ent-kaurene, first step is catalyzed by EC 5.5.1.13 (ent-kaurene synthase A)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ent-copalyl diphosphate = ent-kaurene + diphosphate
-
-
-
-
ent-copalyl diphosphate = ent-kaurene + diphosphate
reaction mechanism, overview
ent-copalyl diphosphate = ent-kaurene + diphosphate
the determination of the final products of CPS/KSs in bryophytes depends on the sequence and structure of the C-terminal regions of CPS/KSs. Thus, the type A cyclization reaction of both PpCPS/KS and JsCPS /KS occurs near the C-terminal region of the polypeptides
-
ent-copalyl diphosphate = ent-kaurene + diphosphate
the hydrophobicity and size of the side chain residue at the bifunctional CPS/KS amino acid 710 is responsible for quenching the ent-kauranyl cation by the addition of a water molecule. The determination of the final products of CPS/KSs in bryophytes depends on the sequence and structure of the C-terminal regions of CPS/KSs. Thus, the type A cyclization reaction of both PpCPS/KS and JsCPS /KS occurs near the C-terminal region of the polypeptides
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
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
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
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
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
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
ent-copalyl diphosphate = ent-kaurene + diphosphate
cyclization mechanism derived from quantum chemical calculation for the formation of ent-kaurene and related diterpenes, overview
ent-copalyl diphosphate = ent-kaurene + diphosphate
reaction mechanism, overview
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
diphosphate lysis
-
-
-
-
cyclization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ent-copalyl-diphosphate diphosphate-lyase (cyclizing, ent-kaurene-forming)
Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase)
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CAS REGISTRY NUMBER
COMMENTARY
9055-64-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8alpha-hydroxy-copalyl diphosphate
ent-13-epi-manoyl oxide + diphosphate
produced by recombinant Arabidopsis thaliana ent-copalyl diphosphate synthase mutant H263A
-
-
?
ent-copalyl diphosphate
16alpha-hydroxykaurane + ent-kaurene + diphosphate
-
-
-
-
?
ent-copalyl diphosphate
ent-isokaur-15-ene + diphosphate
enzyme OsKSL5i, via the ent-kauran-16-yl intermediate, overview
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + 6alpha-hydroxy-ent-kaurane + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-sandaracopimaradiene + diphosphate
-
-
-
?
ent-copalyl diphosphate + H2O
16alpha-hydroxy-ent-kaur-ene + 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
-
-
?
geranylgeranyl diphosphate
ent-kaurene + diphosphate
PpCPS-KS directly synthesizes the ent-kaurene skeleton from GGDP
-
-
?
8beta-hydroxy-ent-copalyl diphosphate
ent-13-epi-manoyl oxide + ent-kaurene + diphosphate
-
-
-
-
?
8beta-hydroxy-ent-copalyl diphosphate
ent-13-epi-manoyl oxide + ent-kaurene + diphosphate
-
-
-
-
?
copalyl diphosphate
sandaracopimaradiene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + 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
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + 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
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
second step in plant hormone gibberellin biosynthesis, regulation of the gibberellin biosynthesis, the KS is not rate-determining, overview
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
Fusarium fujikuroi CBS 195.34 / IMI 58289 / NRRL A-6831
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
-
the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
the enzyme is involved in gibberellin metabolism and biosynthesis of diterpene phytoalexins, overview
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
ent-copalyl diphosphate is converted in an ionization-initiated (class I) reaction that involves formation of a pimarenyl carbocation intermediate, followed by secondary cyclization to a beyeranyl cation which undergoes ring rearrangement and deprotonation to form the tetracyclic ent-kaurene
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
-
additionally an unidentified acid labile compound is formed that is not found in products from pea and pumpkin
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
additionally an unidentified acid labile compound is formed that is not found in products from pea and pumpkin
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate + H2O
16-hydroxy-ent-kaurene + diphosphate
-
-
-
?
ent-copalyl diphosphate + H2O
16-hydroxy-ent-kaurene + diphosphate
-
-
-
-
?
ent-copalyl diphosphate + H2O
16alpha-hydroxy-ent-kaurane + diphosphate
-
-
the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
?
ent-copalyl diphosphate + H2O
16alpha-hydroxy-ent-kaurane + diphosphate
-
the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
?
additional information
?
-
GC-MS analysis of products, overview
-
-
?
additional information
?
-
the ent-copalyl diphosphate substrate binds to a hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the carbocations formed on ionization being protected by Leu, Tyr and Phe residues
-
-
?
additional information
?
-
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
the ent-copalyl diphosphate substrate binds to a hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the carbocations formed on ionization being protected by Leu, Tyr and Phe residues
-
-
?
additional information
?
-
GC-MS analysis of products, overview
-
-
?
additional information
?
-
GC-MS analysis of products, overview
-
-
?
additional information
?
-
the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase, EC 5.5.1.13, and ent-kaurene synthase. Enzyme CPS produces the precursor for several different diterpenes formed by ent-kaurene synthase, i.e. ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene, via three carbocation intermediates, mechanism, overview. PpCPS/KS is a multiproduct enzyme
-
-
?
additional information
?
-
-
the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase, EC 5.5.1.13, and ent-kaurene synthase. Enzyme CPS produces the precursor for several different diterpenes formed by ent-kaurene synthase, i.e. ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene, via three carbocation intermediates, mechanism, overview. PpCPS/KS is a multiproduct enzyme
-
-
?
additional information
?
-
GC-MS analysis of products, overview
-
-
?
additional information
?
-
the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase and ent-kaurene synthase, EC 4.2.3.19
-
-
?
additional information
?
-
-
the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase and ent-kaurene synthase, EC 4.2.3.19
-
-
?
additional information
?
-
the enzyme forms ent-kaurene via 4 consecutive intermediates (i.e. ent-pimarenyl, ent-beyeranyl, ent-trachylobanyl, and ent-kauranyl), three of which can be the precursor for different diterpenes other than ent-kaurene, overview. Enzyme product analysis by GC-MS. No production of ent-beyerene or ent-atiserene by isozymes RcKSL1 and RcKSL2
-
-
?
additional information
?
-
-
the enzyme forms ent-kaurene via 4 consecutive intermediates (i.e. ent-pimarenyl, ent-beyeranyl, ent-trachylobanyl, and ent-kauranyl), three of which can be the precursor for different diterpenes other than ent-kaurene, overview. Enzyme product analysis by GC-MS. No production of ent-beyerene or ent-atiserene by isozymes RcKSL1 and RcKSL2
-
-
?
additional information
?
-
the enzyme prefers normal and syn-copalyl diphosphate over ent-copalyl diphosphate
-
-
?
additional information
?
-
-
the enzyme prefers normal and syn-copalyl diphosphate over ent-copalyl diphosphate
-
-
?
additional information
?
-
GC-MS analysis of products, overview
-
-
?
additional information
?
-
CPS/KS catalyzes the two-step cyclization of geranylgeranyl diphosphate to ent-kaurene via ent-copalyl diphosphate
-
-
?
additional information
?
-
-
CPS/KS catalyzes the two-step cyclization of geranylgeranyl diphosphate to ent-kaurene via ent-copalyl diphosphate
-
-
?
additional information
?
-
CPS/KS catalyzes the two-step cyclization of geranylgeranyl diphosphate to ent-kaurene via ent-copalyl diphosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
copalyl diphosphate
sandaracopimaradiene + diphosphate
-
-
-
?
ent-copalyl diphosphate
16alpha-hydroxykaurane + ent-kaurene + diphosphate
-
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + 6alpha-hydroxy-ent-kaurane + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-sandaracopimaradiene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaur-16-ene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
second step in plant hormone gibberellin biosynthesis, regulation of the gibberellin biosynthesis, the KS is not rate-determining, overview
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
Fusarium fujikuroi CBS 195.34 / IMI 58289 / NRRL A-6831
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
the enzyme is involved in gibberellin metabolism and biosynthesis of diterpene phytoalexins, overview
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
ent-copalyl diphosphate is converted in an ionization-initiated (class I) reaction that involves formation of a pimarenyl carbocation intermediate, followed by secondary cyclization to a beyeranyl cation which undergoes ring rearrangement and deprotonation to form the tetracyclic ent-kaurene
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
additionally an unidentified acid labile compound is formed that is not found in products from pea and pumpkin
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
-
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
-
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate + H2O
16-hydroxy-ent-kaurene + diphosphate
-
-
-
?
ent-copalyl diphosphate + H2O
16-hydroxy-ent-kaurene + diphosphate
-
-
-
-
?
additional information
?
-
the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase, EC 5.5.1.13, and ent-kaurene synthase. Enzyme CPS produces the precursor for several different diterpenes formed by ent-kaurene synthase, i.e. ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene, via three carbocation intermediates, mechanism, overview. PpCPS/KS is a multiproduct enzyme
-
-
?
additional information
?
-
-
the bifunctional diterpene synthase PpCPS/KS catalyzes both the reactions of ent-copalyl diphosphate synthase, EC 5.5.1.13, and ent-kaurene synthase. Enzyme CPS produces the precursor for several different diterpenes formed by ent-kaurene synthase, i.e. ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene, via three carbocation intermediates, mechanism, overview. PpCPS/KS is a multiproduct enzyme
-
-
?
additional information
?
-
the enzyme prefers normal and syn-copalyl diphosphate over ent-copalyl diphosphate
-
-
?
additional information
?
-
-
the enzyme prefers normal and syn-copalyl diphosphate over ent-copalyl diphosphate
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Ni2+
Mg2+
isozyme RcKSL2 contains a significant deviation from the usually well-conserved (N/D)Dxx(S/T)xxxE sequence that serves as a secondary Mg2+ binding motif
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
BPH-629
the bisphosphonate inhibitor binds to a hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the carbocations formed on ionization being protected by Leu, Tyr and Phe residues, enzyme binding structure analysis, overview
additional information
-
wide variety of quaternary ammonium compounds with structural similarities to geranylgeranyl diphosphate tested for inhibition, substances shows significant effects on AB activity, but low effects on B activity
-
2'-isopropyl-4'(trimethylammonium chloride)-5'-methylphenyl piperidine-1-carboxylate
-
Amo-1618; strong inhibition of EC 5.5.1.13 activity, very weak inhibition of EC 4.2.3.19 activity
2'-isopropyl-4'(trimethylammonium chloride)-5'-methylphenyl piperidine-1-carboxylate
Amo-1618
2-(N,N-dimethyl-N-octylammonium bromide)-p-methan-1-ol
-
strong inhibition of EC 5.5.1.13 activity, very weak inhibition of EC 4.2.3.19 activity
AMO-1618
-
i.e. trimethyl-[2-methyl-(4-piperidine-1-carbonyloxy)-5-propan-2-ylphenyl]azonium chloride
copalyl diphosphate
-
slight substrate inhibition at concentrations above 0.0007 mM
copalyl diphosphate
-
substrate inhibition above 0.0002 mM, might be an effect of contaminants in substrate preparations
N,N-dimethylaminoethyl 2,2-diphenylphenylether
-
strong inhibition of EC 5.5.1.13 activity, very weak inhibition of EC 4.2.3.19 activity
Phosphone D
-
strong inhibition of EC 5.5.1.13 activity, very weak inhibition of EC 4.2.3.19 activity
Phosphone S
-
strong inhibition of EC 5.5.1.13 activity, very weak inhibition of EC 4.2.3.19 activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression of KS4, KS7, and KS8 is induced by elicitor treatment
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
[15-3H]ent-copalyl diphosphate
pseudo-binding constant for [15-3H]ent-copalyl diphosphate with GST-recombinant kaurene synthase
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0095
BPH-629
Bradyrhizobium diazoefficiens
pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity in wild-type and trabsgenic KS-overexpressing plants
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19
-
-
brenda
bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
during embryo development, mRNA levels of KS3L peak at an early stage of zygotic embryogenesis
brenda
additional information
the SdKS gene is mainly expressed in the root and lateral root systems, which are elongating tissues, quantitative real-time PCR expression analysis
brenda
-
no activity in fresh crude extracts from seedlings for ent-kaurene formation from geranyl-geranyl diphosphate, activity detected after some days of storage in liquid nitrogen, little effect of liquid nitrogen storage on EC 4.2.3.19 activity
brenda
additional information
KS2L mRNA is undetected in any stage of sunflower embryos
brenda
additional information
KS2L mRNA is undetected in any stage of sunflower embryos
brenda
additional information
relative transcript levels of SdCPS1, SdKS, SdKO1, and SdKO2 are determined in young and mature leaves, upper and lower stems, roots, and lateral roots of Scoparia dulcis
brenda
additional information
-
relative transcript levels of SdCPS1, SdKS, SdKO1, and SdKO2 are determined in young and mature leaves, upper and lower stems, roots, and lateral roots of Scoparia dulcis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
based on the predicted presence of the N-terminal chloroplast transit pepitde
brenda
the enzyme sequence contains a plastid transit peptide sequence, the first 27 N-terminal amino acids rich in serine and threonine (22%)
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
plants have extensively diversified their arsenal of labdane-related diterpenoids (LRDs), in part via gene duplication and neo-functionalization of the ancestral ent-kaurene synthase (KS) required for gibberellin metabolism. Ricinus communis contains 4 RcKSL isozymes, molecular phylogenetic analysis indicates that RcKSL1 is significantly more closely related to dicotyl ent-kaurene synthases (KSs), while the other three, RcKSL2-4, cluster separately. RcKSL2-4 are in close proximity to each other, within a region of 65 kb, with RcKSL2 and 4 occurring as a tandem gene pair. RcKSL1 is the only isozyme to react with ent-CPP producing small amounts of ent-kaurene, and is referred to as RcKS1. Both RcKSL2 and RcKSL3 also are selectively reacting with ent-CPP with RcKSL2 producing primarily ent-trachylobane (70%) as well as smaller amounts of ent-kaurene (30%), and RcKSL3 producing ent-sandaracopimaradiene (94%) (EC 4.2.3.29) along with small amounts of ent-labdatriene (3%) and ent-pimaradiene (3%). RcKSL4 seems to be inactive, with no products evident from any substrate, but upon synthesis of a codon-optimized gene for the corrected aa sequence and functional analysis, RcKSL4 selectively reacts with ent-CPP and produces largely ent-beyerene (95%) along with very small amounts of ent-atiserene (4%) and ent-kaurene (1%). The enzymes belong to the terpene synthase family
evolution
PpCPS/KS is a multiproduct enzyme. It is one of the evolutionary earliest occurring plant diterpene synthases. Thus, PpCPS/KS may have been a multiproduct platform for later evolved diterpene synthases in plants
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
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
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
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
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
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
evolution
the enzyme is a class I bacterial diterpene cyclase
evolution
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
the enzyme is a class I bacterial diterpene cyclase
-
evolution
Fusarium fujikuroi CBS 195.34 / IMI 58289 / NRRL A-6831
-
the enzyme is a class I diterpene cyclase
-
malfunction
CPS/KS disruption mutant lines have defect in protonemal development. The differentiation of chloronemata to caulonemata is suppressed in the CPS/KS knockout mutants
malfunction
CPS/KS disruption mutant lines have defect in protonemal development. The differentiation of chloronemata to caulonemata is suppressed in the CPS/KS knockout mutants
malfunction
-
CPS/KS disruption mutant lines have defect in protonemal development. The differentiation of chloronemata to caulonemata iss suppressed in the CPS/KS knockout mutants
malfunction
caulonemal differentiation in a Physcomitrella patens mutant with a disrupted bifunctional ent-copalyl diphosphate synthase/ent-kaurene synthase (PpCPS/KS) gene is suppressed under red light, and is recovered by application of ent-kaurene and ent-kaurenoic acid. Although avoidance of the blue light source is not observed in the ent-kaurene deficient mutant protonemata, chloronemal growth toward a blue-light source in the mutant is suppressed by application of ent-kaurenoic acid, and the growth is rescued to that in the wild type
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
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
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
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
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
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
metabolism
class I bacterial diterpene cyclase, ent-kaurene synthase (BjKS) catalyzes the cyclization of ent-copalyl diphosphate (ent-CPP), which is produced by the separate (class II) enzyme, ent-copalyl diphosphate synthase (ent-CPPS, EC 5.5.1.13) from geranylgeranyl diphosphate, to ent-kaurene
metabolism
gibberellins (GAs) are ubiquitous diterpenoids in higher plants, whereas some higher plants produce unique species-specific diterpenoids. In gibberellins biosynthesis, ent-kaurene synthase and ent-kaurene oxidase are key players which catalyze early step(s) of the cyclization and oxidation reactions
metabolism
the enzyme catalyzes a step in the gibberellin biosynthetic pathway. The tanshinone biosynthetic pathway is uniquely initiated by a sequential pair of cyclization reactions catalyzed by SmCPS1 and SmKSL1 to produce abietane miltiradiene. Enzyme SmCPSent catalyzes the cyclization of geranylgeranyl diphosphate to ent-copalyl diphosphate (ent-CPP), which is converted to ent-kaurene by ent-kaurene synthase, SmKS. ent-Kaurene oxidase (SmKO) then catalyzes the three-step oxidation of ent-kaurene to ent-kaurenoic acid
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)
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)
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)
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)
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)
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)
metabolism
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
class I bacterial diterpene cyclase, ent-kaurene synthase (BjKS) catalyzes the cyclization of ent-copalyl diphosphate (ent-CPP), which is produced by the separate (class II) enzyme, ent-copalyl diphosphate synthase (ent-CPPS, EC 5.5.1.13) from geranylgeranyl diphosphate, to ent-kaurene
-
physiological function
-
enzyme overexpression results in elevated gibberellic acid production
physiological function
copalyl diphosphate/kaurene synthase from the moss Physcomitrella patens (PpCPS/KS) is a bifunctional diterpene synthase and catalyses the formation of at least four diterpenes, including ent-beyerene, ent-sandaracopimaradiene, ent-kaur-16-ene, and 16-hydroxy-ent-kaurene
physiological function
ent-copalyl diphosphate (ent-CPP) is produced by the separate (class II) enzyme, ent-copalyl diphosphate synthase (ent-CPPS, EC 5.5.1.13), from geranylgeranyl diphosphate. The ent-kaur-16-ene synthase then catalyzes the cyclization of ent-copalyl diphosphate (ent-CPP) to ent-kaurene
physiological function
enzyme SdKS catalyzes a cyclization reaction from ent-copalyl diphosphate to ent-kaurene and is a key enzyme in the gibberellins biosynthesis
physiological function
geranylgeranyl diphosphate (GGPP) is an essential precursor in the biosynthesis of several diterpenes including ent-kaurene via formation of ent-copalyl diphosphate. Effect of isoprenoid precursors on ent-copalyl diphosphate and ent-kaurene production, ent-kaurene is quantified using GC-MS analysis
physiological function
plants have extensively diversified their arsenal of labdane-related diterpenoids (LRDs), in part via gene duplication and neo-functionalization of the ancestral ent-kaurene synthase (KS) required for gibberellin metabolism
physiological function
-
the enzyme is involved in defense mechanisms in rice roots
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
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
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
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
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
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
physiological function
the moss Physcomitrella patens possesses parts of the gibberellins biosynthetic pathway, from geranylgeranyl diphosphate to ent-kaurenoic acid, but no gibberellins are found in this species. Derivatives of ent-kaurenoic acid, not gibberellins, might act as endogenous developmental regulators. Blue light regulates ent-kaurene biosynthesis and avoidance response to protonemal growth. When protonemata of the wild-type plants are incubated under blue light, the chloronemal filaments grow in the opposite direction to the light source. Regulators derived from ent-kaurenoic acid are strongly involved not only in the growth regulation of caulonemal differentiation under red light, but also in the light avoidance response of chloronemal growth under blue light. In particular, growth under blue light is regulated via the PpCPS/KS gene
physiological function
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
ent-copalyl diphosphate (ent-CPP) is produced by the separate (class II) enzyme, ent-copalyl diphosphate synthase (ent-CPPS, EC 5.5.1.13), from geranylgeranyl diphosphate. The ent-kaur-16-ene synthase then catalyzes the cyclization of ent-copalyl diphosphate (ent-CPP) to ent-kaurene
-
additional information
the enzyme amino acid sequence contains a DDFFD motif but lacks the DxDD motif, indicating that SmKS is a plant KS protein with monofunctional class I diTPS activity
additional information
-
the enzyme amino acid sequence contains a DDFFD motif but lacks the DxDD motif, indicating that SmKS is a plant KS protein with monofunctional class I diTPS activity
additional information
the enzyme contains the highly conserved DDXXD sequence
additional information
the hydroxyl group of the Thr638 side chain enables occasional addition of water
additional information
the hydroxyl group of the Thr664 side chain enables occasional addition of water
additional information
the production of manoyl oxide proceeds from a substrate wherein oxygen is already present in the form of a hydroxyl group added during bicyclization of the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) to 8alpha-hydroxy-copalyl diphosphate catalysed by recombinant Arabidopsis thaliana ent-copalyl diphosphate synthase mutant H263A, EC 5.5.1.13. 8alpha-Hydroxy-copalyl diphosphate is then converted to ent-13-epi-manoyl oxide by the modified ent-kaurene synthase function of enzyme FfCPS/KS mutant H212A
additional information
-
the production of manoyl oxide proceeds from a substrate wherein oxygen is already present in the form of a hydroxyl group added during bicyclization of the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) to 8alpha-hydroxy-copalyl diphosphate catalysed by recombinant Arabidopsis thaliana ent-copalyl diphosphate synthase mutant H263A, EC 5.5.1.13. 8alpha-Hydroxy-copalyl diphosphate is then converted to ent-13-epi-manoyl oxide by the modified ent-kaurene synthase function of enzyme PpCPS/KS mutant H302A
additional information
the production of manoyl oxide proceeds from a substrate wherein oxygen is already present in the form of a hydroxyl group added during bicyclization of the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) to 8alpha-hydroxy-copalyl diphosphate catalysed by recombinant Arabidopsis thaliana ent-copalyl diphosphate synthase mutant H263A, EC 5.5.1.13. 8alpha-Hydroxy-copalyl diphosphate is then converted to ent-13-epi-manoyl oxide by the modified ent-kaurene synthase function of enzyme PpCPS/KS mutant H302A
additional information
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
the enzyme contains the highly conserved DDXXD sequence
-
additional information
Fusarium fujikuroi CBS 195.34 / IMI 58289 / NRRL A-6831
-
the production of manoyl oxide proceeds from a substrate wherein oxygen is already present in the form of a hydroxyl group added during bicyclization of the general diterpenoid precursor (E,E,E)-geranylgeranyl diphosphate (GGPP) to 8alpha-hydroxy-copalyl diphosphate catalysed by recombinant Arabidopsis thaliana ent-copalyl diphosphate synthase mutant H263A, EC 5.5.1.13. 8alpha-Hydroxy-copalyl diphosphate is then converted to ent-13-epi-manoyl oxide by the modified ent-kaurene synthase function of enzyme FfCPS/KS mutant H212A
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TPS4_VITAC
789
0
90215
Swiss-Prot
Mitochondrion (Reliability: 4)
GA6_GIBF5
Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831)
952
0
106762
Swiss-Prot
other Location (Reliability: 2)
CPSKS_GIBFU
952
0
106804
Swiss-Prot
other Location (Reliability: 2)
CPSKS_PHASA
Phaeosphaeria sp. (strain L487)
946
0
105724
Swiss-Prot
other Location (Reliability: 2)
EKS_MARVU
756
0
86373
Swiss-Prot
other Location (Reliability: 3)
KSL5_ISORU
794
0
90379
Swiss-Prot
Mitochondrion (Reliability: 4)
KSB_ARATH
785
0
89622
Swiss-Prot
Chloroplast (Reliability: 3)
KSB_CUCMA
789
0
89362
Swiss-Prot
Mitochondrion (Reliability: 4)
KSB_SALMI
806
0
92156
Swiss-Prot
Chloroplast (Reliability: 3)
KS1_ISOER
794
0
90262
Swiss-Prot
Mitochondrion (Reliability: 4)
KS1_ORYSJ
756
0
85959
Swiss-Prot
Mitochondrion (Reliability: 5)
KS1_STERE
784
0
89402
Swiss-Prot
Chloroplast (Reliability: 5)
KS2_STERE
784
0
89401
Swiss-Prot
Chloroplast (Reliability: 5)
B9SIM3_RICCO
775
0
88179
TrEMBL
other Location (Reliability: 3)
A0A8F2T9R1_CHAFM
834
0
95732
TrEMBL
Mitochondrion (Reliability: 4)
A0A0B2QJ52_GLYSO
792
0
90553
TrEMBL
other Location (Reliability: 5)
A0A2P6SGZ2_ROSCH
373
0
42414
TrEMBL
other Location (Reliability: 4)
A0A2P6SGC2_ROSCH
302
0
34214
TrEMBL
other Location (Reliability: 3)
A0A8F2PHW2_CHAFM
856
0
98518
TrEMBL
Mitochondrion (Reliability: 3)
A0A5B7ATW7_DAVIN
468
0
53620
TrEMBL
other Location (Reliability: 3)
D0Q1D5_COFAR
808
0
92531
TrEMBL
Mitochondrion (Reliability: 3)
A0A2G9GGI4_9LAMI
372
0
42428
TrEMBL
other Location (Reliability: 5)
G7JC43_MEDTR
384
0
43978
TrEMBL
other Location (Reliability: 4)
B9SIL7_RICCO
816
1
93570
TrEMBL
Mitochondrion (Reliability: 5)
A0A2I0A9M4_9ASPA
790
0
90008
TrEMBL
Chloroplast (Reliability: 3)
A0A7C9A407_OPUST
170
0
19397
TrEMBL
Mitochondrion (Reliability: 5)
D4IIJ1_HELAN
772
0
88015
TrEMBL
Chloroplast (Reliability: 5)
A0A2P6SGE7_ROSCH
376
0
42535
TrEMBL
other Location (Reliability: 4)
A0A2P6SGZ5_ROSCH
375
0
42532
TrEMBL
other Location (Reliability: 4)
A0A2G9GSV5_9LAMI
564
0
64943
TrEMBL
Mitochondrion (Reliability: 5)
U5YN00_MALDO
737
0
83477
TrEMBL
other Location (Reliability: 3)
B9T888_RICCO
408
0
47635
TrEMBL
other Location (Reliability: 2)
A0A2P6Q831_ROSCH
799
0
90138
TrEMBL
Chloroplast (Reliability: 4)
A0A2G9GJY2_9LAMI
367
0
41881
TrEMBL
other Location (Reliability: 3)
A0A2G9I3V3_9LAMI
383
0
43610
TrEMBL
other Location (Reliability: 5)
B9T625_RICCO
808
0
92020
TrEMBL
other Location (Reliability: 3)
A0A0R7FFR3_9MAGN
743
0
84987
TrEMBL
other Location (Reliability: 3)
A0A2P6Q833_ROSCH
522
0
59687
TrEMBL
Chloroplast (Reliability: 5)
D2XEB3_PICGL
757
0
87280
TrEMBL
other Location (Reliability: 1)
A0A2G9GSX0_9LAMI
631
0
72542
TrEMBL
other Location (Reliability: 3)
A0A220NVF3_CAMSI
791
0
89709
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B2SQ17_GLYSO
836
0
96073
TrEMBL
other Location (Reliability: 3)
B9S5Y1_RICCO
335
0
38714
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SGD9_ROSCH
376
0
42707
TrEMBL
other Location (Reliability: 3)
A0A2P6Q826_ROSCH
102
0
11325
TrEMBL
other Location (Reliability: 5)
A0A8F2PTV9_CHAFM
749
0
86293
TrEMBL
Mitochondrion (Reliability: 5)
A0A396J8H5_MEDTR
799
0
90957
TrEMBL
Chloroplast (Reliability: 4)
A0A2G9H326_9LAMI
362
0
41305
TrEMBL
other Location (Reliability: 4)
A0A2P6PMX0_ROSCH
351
0
40575
TrEMBL
other Location (Reliability: 2)
A0A8F2PKC2_CHAFM
847
0
97668
TrEMBL
Chloroplast (Reliability: 3)
B9T8C9_RICCO
408
0
47838
TrEMBL
other Location (Reliability: 3)
A0A8F2TA91_CHAFM
859
0
98190
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B2PDG5_GLYSO
167
0
19094
TrEMBL
other Location (Reliability: 3)
B9SIM2_RICCO
778
0
88764
TrEMBL
other Location (Reliability: 5)
A0A5B7AS58_DAVIN
702
0
80191
TrEMBL
Chloroplast (Reliability: 4)
A0A072VM18_MEDTR
376
0
42965
TrEMBL
other Location (Reliability: 2)
A0A072V0R4_MEDTR
362
0
41428
TrEMBL
other Location (Reliability: 2)
A0A2P6Q089_ROSCH
373
0
41749
TrEMBL
Chloroplast (Reliability: 5)
A0A2P6Q847_ROSCH
724
0
81881
TrEMBL
other Location (Reliability: 2)
A0A2G9GNY5_9LAMI
384
0
43823
TrEMBL
other Location (Reliability: 3)
D4IIJ0_HELAN
774
0
87993
TrEMBL
Chloroplast (Reliability: 5)
A0A072UX51_MEDTR
800
0
91608
TrEMBL
Chloroplast (Reliability: 4)
B9T8D0_RICCO
161
0
18627
TrEMBL
Mitochondrion (Reliability: 5)
A0A176VPW0_MARPO
749
0
85108
TrEMBL
-
Y2150_BRADU
Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
300
0
33380
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106000
copalyl diphosphate synthase-kaurene synthase fusion protein, determined by SDS-PAGE and Western blot analysis
131000
-
molecular weight of cloned fusion protein predicted from DNA sequence
81000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme structure comparisons, overview
additional information
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
enzyme structure comparisons, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the enzyme sequence contains a plastid transit peptide sequence, which is cleaved off for enzyme maturation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme in apo form or in complex with inhibitor BPH-629, mutant D75C in complex with substrate ent-copalyl diphosphate, sitting drop vapor diffusion method, mixing of 6.4 mg/ml protein in 25 mM Tris, pH 7.5, and 150 mM NaCl with reservoir solution containing 0.7 M ammonium tartrate dibasic, pH 7.0 and 2-4% w/v PEG 4000 for the wild-type enzyme, for the inhibitor BPH-629 complex, the enzyme solution also contains 1 mM MgCl2, 10 mM DTT, and 2.5 mM BPH-629, for the substrate complex, the D75C mutant crystal is prepared under the same crystallization conditions, then soaked with the cryo-protectant containing 5 mM ent-copalyl diphosphate for 5 hours, 2-3 days, room temperature, X-ray diffraction structure determination and analysis at 1.80-2.34 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
I368S
the mutant produces ent-pimara-8(14),15-diene and 8alpha-hydroxy-ent-pimara-15-ene from ent-copalyl diphosphate
I368T
the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate
I368V
the mutant produces ent-kaur-16-ene from ent-copalyl diphosphate
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
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
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
I638V
site-directed mutagenesis, the mutant shows unaltered product spectrum compared to the wild-type enzyme and produces just ent-kaur-16-ene
D75C
site-directed mutagenesis, mutant crystal structure determination and analysis
D75A
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
site-directed mutagenesis
-
D75C
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
site-directed mutagenesis, mutant crystal structure determination and analysis
-
D79C
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
site-directed mutagenesis
-
R204A
Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110
-
site-directed mutagenesis
-
H212A
I645T
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
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
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
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
A710C
no change in reaction product profile compared to wild-type
A710F
mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product
A710G
no change in reaction product profile compared to wild-type
A710M
mutant converted geranylgeranyl diphosphate to ent-kaurene as the sole product
A710N
no change in reaction product profile compared to wild-type
A710S
no change in reaction product profile compared to wild-type
D635A/D636A
mutation of the DDYFD motif in the kaurene synthase domain
H302A
I741T
I619A
site-directed mutagenesis, the mutant shows altered product spectrum compared to the wild-type enzyme
A676T
site-directed mutagenesis of isozyme RcKSL2, mutation of the catalytically important residue results in 60fold increased product amount composed of essentially the same mix of ent-trachylobane and ent-kaurene as observed for the wild-type enzyme
additional information
H212A
the mutant shows altered substrate specificity compared to wild-type, the single histidine to alanine mutation converts FfCPS/KS into a bifunctional ent-13-epi-manoyl oxide synthase
H212A
Fusarium fujikuroi CBS 195.34 / IMI 58289 / NRRL A-6831
-
the mutant shows altered substrate specificity compared to wild-type, the single histidine to alanine mutation converts FfCPS/KS into a bifunctional ent-13-epi-manoyl oxide synthase
-
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
I645T
the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate
H302A
the mutant efficiently produces ent-13-epi-manoyl oxide from geranylgeranyl diphosphate
H302A
the mutant shows altered substrate specificity compared to wild-type, the single histidine to alanine mutation converts PpCPS/KS into a bifunctional ent-13-epi-manoyl oxide synthase
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
I741T
the mutant produces ent-pimara-8(14),15-diene from ent-copalyl diphosphate
additional information
-
construction of transgenic Arabidopsis thaliana plants, using the Agrobacterium tumefaciens infection system, overexpressing KS leads to increased ent-kaurene production but not to an increase in bioactive gibberellins, no altered morphology or phenotype compared to wild-type plants
additional information
-
construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-86 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
-
construction of transgenic rice mutants expressing mutated KS-like genes, the mutant plants show reduced enzyme activity, phenotype analysis and effects on gibberellin metabolism, overview
additional information
several N- and C-terminal truncated enzymes produced, all found to be inactive
additional information
-
several N- and C-terminal truncated enzymes produced, all found to be inactive
additional information
construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-886 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
-
construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-886 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
generation of a Physcomitrella patens CPS/KS (PpCPS/KS)-gene disruption mutant strain A74, comparisons of photomorphogenesis of protonema in the wild-type and the A74 enzyme mutant, phenotype, detailed overview
additional information
-
generation of a Physcomitrella patens CPS/KS (PpCPS/KS)-gene disruption mutant strain A74, comparisons of photomorphogenesis of protonema in the wild-type and the A74 enzyme mutant, phenotype, detailed overview
additional information
construction of a SmKS-SmCPSent fusion enzyme (CPSent is ent-copalyl diphosphate synthase, EC 5.5.1.13), which improves the ent-kaurene precursor supply in transformed Saccharomyces cerevisiae strain SGH5 (BY-T20/pESC-Trp::SmKS-SmCPSent/SmKO + pESC-Leu::SmCPR1)
additional information
-
construction of a SmKS-SmCPSent fusion enzyme (CPSent is ent-copalyl diphosphate synthase, EC 5.5.1.13), which improves the ent-kaurene precursor supply in transformed Saccharomyces cerevisiae strain SGH5 (BY-T20/pESC-Trp::SmKS-SmCPSent/SmKO + pESC-Leu::SmCPR1)
additional information
-
a synthetic ent-kaurene module, expressing Stevia rebaudiana CPPS and KS, and Rhodobacter sphaeroides GGPPS (crtE gene), is constructed for ent-kaurene production in diverse Escherichia coli strains, best in strain MG1655, method optimization, several crtE genes from Rhodobacter species are validated, overview
additional information
a synthetic ent-kaurene module, expressing Stevia rebaudiana CPPS and KS, and Rhodobacter sphaeroides GGPPS (crtE gene), is constructed for ent-kaurene production in diverse Escherichia coli strains, best in strain MG1655, method optimization, several crtE genes from Rhodobacter species are validated, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no activity in fresh crude extracts from seedlings for ent-kaurene formation from geranyl-geranyl diphosphate, activity detected after some days of storage in liquid nitrogen, little effect of liquid nitrogen storage on EC 4.2.3.19 activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-180°C, no activity in fresh crude extracts from seedlings for ent-kaurene formation from geranyl-geranyl diphosphate, activity detected after some days of storage in liquid nitrogen, little effect of liquid nitrogen storage on EC 4.2.3.19 activity
-
-20°C, 25% glycerol, several months, no loss of activity for purified enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap nickel-affinity column chromatography
Ni-NTA column chromatography
partial, copurified with ent-kaurene synthase A (EC 5.5.1.13) activity
-
recombinant thioredoxin- and His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21trxB (DE3) by nickel affinity chromatography, followed by tag cleavage by TEV protease, another step of nickel affinity chromatography, anion exchange chromatography, and ultrafiltration
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3)
recombinant wild-type enzyme from Escherichia coli strain C41(DE3)
separation of activities A and B achieved by hydrophobic interaction chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3)
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3)
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3)
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3)
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination of genes KS1-9, chromosomal localizations, gene KS9 is a pseudogene, phylogenetic analysis, overview
-
expressed in Escherichia coli as fusion protein with maltose-binding protein, enzyme exclusively shows EC 4.2.3.19 activity
-
expressed in Escherichia coli C41 cells
expressed in Escherichia coli JM109 as glutathione-S-transferase fusion protein, enzyme shows EC 4.2.3.19 and EC 5.5.1.13 activity
expressed in Escherichia coli JM109, enzyme shows EC 4.2.3.19 and EC 5.5.1.13 activity
expressed in Escherichia coli OverExpress C41 cells
gene KS, phylogenetic tree, quantitative real-time PCR expression analysis, functional recombinant expression in Escherichia coli strain C41(DE3), GC-MS analysis of diterpene products from hexane extracts of recombinant Escherichia coli harboring the pSdGGeC and pSdKS vectors
gene KS1, a synthetic ent-kaurene module, expressing Stevia rebaudiana CPPS and KS, and Rhodobacter sphaeroides GGPPS (crtE gene), is constructed for ent-kaurene production in diverse Escherichia coli strains, best in strain MG1655
gene PHYPA_009773, quantitative real-time PCR and semiquantitative RT-PCR enzyme expression analysis
gene PHYPA_009773, recombinant expression in Escherichia coli strain C41, transient expression of PpCPSKS with the suppressor of silencing P19 in leafs of 4-weeks-old Nicotiana benthamiana via Agrobacterium tumefaciens strain AGL-1 mediated transformation
into the pTD1 vector as a fusion of copalyl diphosphate synthase and ent-kaurene synthase for in vitro expression
isozyme determination and phylogenetic analysis and tree, sequence comparisons, overview. Synthetic RcKS(L) isozymes are truncated to remove the N-terminal plastid-directing transit peptide sequences, they are individually subcloned into compatible expression vectors and each coexpressed with either the geranylgeranyl phosphate synthase (GGPS), or the GGPS along with a CPS (EC 5.5.1.13) for recombinant expression in Escherichia coli
overexpression of CPS and KS in transgenic Arabidopsis thaliana plants, expression in Escherichia coli
-
recombinant expression of enzyme mutant H302A in Escherichia coli
recombinant expression of thioredoxin- and His-tagged wild-type and mutant enzymes with or without selenium-methionine labeling in Escherichia coli strain BL21trxB (DE3)
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
sequence comparisons, recombinant expression of wild-type enzyme in Escherichia coli strain C41(DE3)
SmKS DNA and amino acid sequence determination and analysis of full-length enzyme from cDNA, sequence comparisons and phylogenetic analysis and tree, recombinant enzyme expression in Saccharomyces cerevisiae strain BY-T20
expressed in Escherichia coli OverExpress C41 cells
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression analysis of the PpCPS/KS gene shows that the mRNA level under blue light is rapidly increased and is five times higher than under red light, comparisons of photomorphogenesis of protonema in the wild-type and the A74 enzyme mutant
kaurene synthase-like 2 is drastically induced in roots by 0.1 mM methyl jasmonate treatment
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fall, R.R.; West, C.A.
Purification and properties of kaurene synthetase from Fusarium moniliforme
J. Biol. Chem.
246
6913-6928
1971
Fusarium verticillioides
brenda
Yamaguchi, S.; Saito, T.; Abe, H.; Yamane, H.; Murofushi, N.; Kamiya, Y.
Molecular cloning and characterization of a cDNA encoding the gibberellin biosynthetic enzyme ent-kaurene synthase B from pumpkin (Cucurbita maxima L.)
Plant J.
10
203-213
1996
Cucurbita maxima
brenda
Kawaide, H.; Imai, R.; Sassa, T.; Kamiya, Y.
ent-Kaurene synthetase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis
J. Biol. Chem.
272
21706-21712
1997
Phaeosphaeria sp. (O13284), Phaeosphaeria sp., Phaeosphaeria sp. L487 (O13284)
brenda
Toyomasu, T.; Kawaide, H.; Ishizaki, A.; Shinoda, S.; Otsuka, M.; Mitsuhashi, W.; Sassa, T.
Cloning of a full-length cDNA encoding ent-kaurene synthase from Gibberella fujikuroi: functional analysis of a bifunctional diterpene cyclase
Biosci. Biotechnol. Biochem.
64
660-664
2000
Fusarium fujikuroi (Q9UVY5), Fusarium fujikuroi
brenda
Frost, R.G.; West, C.A.
Properties of kaurene synthetase from Marah macrocarpus
Plant Physiol.
59
22-29
1977
Marah macrocarpa
brenda
Duncan, J.D.; West, C.A.
Properties of kaurene synthetase from Marah macrocarpus endosperm: evidence for the participation of separate but interacting enzymes
Plant Physiol.
68
1128-1134
1981
Marah macrocarpa
brenda
Shen-Miller, J.; West, C.A.
Kaurene synthetase activity in Helianthus annuus. Increases in enzyme activity after storage of seedlings in liquid nitrogen
Plant Physiol.
74
439-441
1984
Helianthus annuus, Marah macrocarpa
brenda
Shen-Miller, J.; West, C.A.
Distribution and ent-kaurene synthetase in Helianthus annuus and Marah macrocarpus
Phytochemistry
24
461-464
1985
Helianthus annuus, Marah macrocarpa
-
brenda
Aach, H.; Boese, G.; Graebe, J.E.
ent-Kaurene biosynthesis in a cell-free system from wheat (Triticum aestivum L.) seedlings and the localization of ent-kaurene synthetase in plastids of three species
Planta
197
333-342
1995
Cucurbita maxima, Pisum sativum, Triticum aestivum
-
brenda
Saito, T.; Abe, H.; Yamane, H.; Sakurai, A.; Murofushi, N.; Takio, K.; Takahashi, N.; Kamiya, Y.
Purification and properties of ent-kaurene synthase B from immature seeds of pumpkin
Plant Physiol.
109
1239-1245
1995
Cucurbita maxima
brenda
Saito, T.; Yamane, H.; Sakurai, A.; Murofushi, N.; Takahashi, N.; Kamiya, Y.
Inhibition of ent-kaurene synthase by quaternary ammonium growth retardants
Biosci. Biotechnol. Biochem.
60
1040-1042
1996
Cucurbita maxima, Fusarium fujikuroi
-
brenda
Aach, H.; Bode, H.; Robinson, D.G.; Graebe, J.E.
ent-Kaurene synthase is located in proplastids of meristematic shoot tissues
Planta
202
211-219
1997
Pisum sativum, Triticum aestivum
-
brenda
Kawaide, H.; Sassa, T.; Kamiya, Y.
Functional analysis of the two interacting cyclase domains in ent-kaurene synthase from the fungus Phaeosphaeria sp. L487 and a comparison with cyclases from higher plants
J. Biol. Chem.
275
2276-2280
2000
Phaeosphaeria sp. (O13284), Phaeosphaeria sp., Phaeosphaeria sp. L487 (O13284)
brenda
Sakamoto, T.; Miura, K.; Itoh, H.; Tatsumi, T.; Ueguchi-Tanaka, M.; Ishiyama, K.; Kobayashi, M.; Agrawal, G.K.; Takeda, S.; Abe, K.; Miyao, A.; Hirochika, H.; Kitano, H.; Ashikari, M.; Matsuoka, M.
An overview of gibberellin metabolism enzyme genes and their related mutants in rice
Plant Physiol.
134
1642-1653
2004
Oryza sativa
brenda
Fleet, C.M.; Yamaguchi, S.; Hanada, A.; Kawaide, H.; David, C.J.; Kamiya, Y.; Sun, T.P.
Overexpression of AtCPS and AtKS in Arabidopsis confers increased ent-kaurene production but no increase in bioactive gibberellins
Plant Physiol.
132
830-839
2003
Arabidopsis thaliana
brenda
Hayashi, K.; Kawaide, H.; Notomi, M.; Sakigi, Y.; Matsuo, A.; Nozaki, H.
Identification and functional analysis of bifunctional ent-kaurene synthase from the moss Physcomitrella patens
FEBS Lett.
580
6175-6181
2006
Physcomitrium patens (A5A8G0), Physcomitrium patens
brenda
Roy, A.; Roberts, F.G.; Wilderman, P.R.; Zhou, K.; Peters, R.J.; Coates, R.M.
16-Aza-ent-beyerane and 16-Aza-ent-trachylobane: potent mechanism-based inhibitors of recombinant ent-kaurene synthase from Arabidopsis thaliana
J. Am. Chem. Soc.
129
12453-12460
2007
Arabidopsis thaliana (Q9SAK2), Arabidopsis thaliana
brenda
Boemke, C.; Rojas, M.C.; Gong, F.; Hedden, P.; Tudzynski, B.
Isolation and characterization of the gibberellin biosynthetic gene cluster in Sphaceloma manihoticola
Appl. Environ. Microbiol.
74
5325-5339
2008
Sphaceloma manihoticola (B5DBY7), Sphaceloma manihoticola, Sphaceloma manihoticola Lu949 (B5DBY7)
brenda
Hayashi, Y.; Toyomasu, T.; Hirose, Y.; Onodera, Y.; Mitsuhashi, W.; Yamane, H.; Sassa, T.; Dairi, T.
Comparison of the enzymatic properties of ent-copalyl diphosphate-synthases in the biosynthesis of phytoalexins and gibberellins in rice
Biosci. Biotechnol. Biochem.
72
523-530
2008
Oryza sativa
brenda
Morrone, D.; Chambers, J.; Lowry, L.; Kim, G.; Anterola, A.; Bender, K.; Peters, R.J.
Gibberellin biosynthesis in bacteria: separate ent-copalyl diphosphate and ent-kaurene synthases in Bradyrhizobium japonicum
FEBS Lett.
583
475-480
2009
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
brenda
Hayashi, K.I.; Horie, K.; Hiwatashi, Y.; Kawaide, H.; Yamaguchi, S.; Hanada, A.; Nakashima, T.; Nakajima, M.; Mander, L.N.; Yamane, H.; Hasebe, M.; Nozaki, H.
Endogenous diterpenes derived from ent-kaurene, a common gibberellin precursor, regulate protonema differentiation of the moss Physcomitrella patens
Plant Physiol.
153
1085-1097
2010
Physcomitrium patens, Picea glauca (D2X8G1), Picea sitchensis (D2X8G3)
brenda
Anterola, A.; Shanle, E.; Mansouri, K.; Schuette, S.; Renzaglia, K.
Gibberellin precursor is involved in spore germination in the moss Physcomitrella patens
Planta
229
1003-1007
2009
Physcomitrium patens
brenda
Pugliesi, C.; Fambrini, M.; Salvini, M.
Molecular cloning and expression profile analysis of three sunflower (Helianthus annuus) diterpene synthase genes
Biochem. Genet.
49
46-62
2011
Helianthus annuus (D4IIJ0), Helianthus annuus (D4IIJ1)
brenda
Kawaide, H.; Hayashi, K.; Kawanabe, R.; Sakigi, Y.; Matsuo, A.; Natsume, M.; Nozaki, H.
Identification of the single amino acid involved in quenching the ent-kauranyl cation by a water molecule in ent-kaurene synthase of Physcomitrella patens
FEBS J.
278
123-133
2011
Liochlaena subulata, Physcomitrium patens (A5A8G0), Physcomitrium patens
brenda
Albermann, S.; Linnemannstoens, P.; Tudzynski, B.
Strategies for strain improvement in Fusarium fujikuroi: overexpression and localization of key enzymes of the isoprenoid pathway and their impact on gibberellin biosynthesis
Appl. Microbiol. Biotechnol.
97
2979-2995
2013
Fusarium fujikuroi
brenda
Shimane, M.; Ueno, Y.; Morisaki, K.; Oogami, S.; Natsume, M.; Hayashi, K.I.; Nozaki, H.; Kawaide, H.
Molecular evolution of the substrate specificity of ent-kaurene synthases to adapt to gibberellin biosynthesis in land plants
Biochem. J.
462
539-546
2014
Selaginella moellendorffii (A0A077JGG8), Selaginella moellendorffii
brenda
Jackson, A.J.; Hershey, D.M.; Chesnut, T.; Xu, M.; Peters, R.J.
Biochemical characterization of the castor bean ent-kaurene synthase(-like) family supports quantum chemical view of diterpene cyclization
Phytochemistry
103
13-21
2014
Ricinus communis (B9T625), Ricinus communis
brenda
Zerbe, P.; Chiang, A.; Bohlmann, J.
Mutational analysis of white spruce (Picea glauca) ent-kaurene synthase (PgKS) reveals common and distinct mechanisms of conifer diterpene synthases of general and specialized metabolism
Phytochemistry
74
30-39
2012
Picea glauca
brenda
Zhou, K.; Xu, M.; Tiernan, M.; Xie, Q.; Toyomasu, T.; Sugawara, C.; Oku, M.; Usui, M.; Mitsuhashi, W.; Chono, M.; Chandler, P.M.; Peters, R.J.
Functional characterization of wheat ent-kaurene(-like) synthases indicates continuing evolution of labdane-related diterpenoid metabolism in the cereals
Phytochemistry
84
47-55
2012
Hordeum vulgare, Triticum aestivum (G9M5S9)
brenda
Zerbe, P.; Rodriguez, S.M.; Mafu, S.; Chiang, A.; Sandhu, H.K.; ONeil-Johnson, M.; Starks, C.M.; Bohlmann, J.
Exploring diterpene metabolism in non-model species transcriptome-enabled discovery and functional characterization of labda-7,13E-dienyl diphosphate synthase from Grindelia robusta
Plant J.
83
783-793
2015
Grindelia hirsutula (A0A0H4SPM5), Grindelia hirsutula
brenda
Yamamura, Y.; Taguchi, Y.; Ichitani, K.; Umebara, I.; Ohshita, A.; Kurosaki, F.; Lee, J.B.
Characterization of ent-kaurene synthase and kaurene oxidase involved in gibberellin biosynthesis from Scoparia dulcis
J. Nat. Med.
72
456-463
2018
Scoparia dulcis (F6M9X0), Scoparia dulcis
brenda
Su, P.; Tong, Y.; Cheng, Q.; Hu, Y.; Zhang, M.; Yang, J.; Teng, Z.; Gao, W.; Huang, L.
Functional characterization of ent-copalyl diphosphate synthase, kaurene synthase and kaurene oxidase in the Salvia miltiorrhiza gibberellin biosynthetic pathway
Sci. Rep.
6
23057
2016
Salvia miltiorrhiza (A0A0U4CDK4), Salvia miltiorrhiza
brenda
Mukherjee, A.
Computational study of a bifunctional ent-kaurene synthase from Physcomitrella patens (Hedw.) Bruch and Schimp. An insight into the origin of terpenoid biosynthesis in plants
Acta Bot. Gallica
162
139-152
2015
Physcomitrium patens
-
brenda
Tezuka, D.; Ito, A.; Mitsuhashi, W.; Toyomasu, T.; Imai, R.
The rice ent-kaurene synthase like 2 encodes a functional ent-beyerene synthase
Biochem. Biophys. Res. Commun.
460
766-771
2015
Oryza sativa
brenda
Mafu, S.; Potter, K.C.; Hillwig, M.L.; Schulte, S.; Criswell, J.; Peters, R.J.
Efficient heterocyclisation by (di)terpene synthases
Chem. Commun. (Camb.)
51
13485-13487
2015
Arabidopsis thaliana, Oryza sativa, Physcomitrium patens, Physcomitrium patens (A5A8G0), Sinorhizobium fredii, Fusarium fujikuroi (S0EA85), Fusarium fujikuroi CBS 195.34 / IMI 58289 / NRRL A-6831 (S0EA85)
brenda
Jia, M.; Peters, R.J.
Extending a single residue switch for abbreviating catalysis in plant ent-kaurene synthases
Front. Plant Sci.
7
1765
2016
Selaginella moellendorffii (A0A077JGG8), Marchantia polymorpha subsp. ruderalis (A0A176VPW0), Physcomitrium patens (A5A8G0), Picea glauca (D2XEB3), Oryza sativa Japonica Group (Q0JA82), Arabidopsis thaliana (Q9SAK2)
brenda
Kong, M.K.; Kang, H.J.; Kim, J.H.; Oh, S.H.; Lee, P.C.
Metabolic engineering of the Stevia rebaudiana ent-kaurene biosynthetic pathway in recombinant Escherichia coli
J. Biotechnol.
214
95-102
2015
Stevia rebaudiana, Stevia rebaudiana (Q9XEH9)
brenda
Jackson, A.; Hershey, D.; Chesnut, T.; Xu, M.; Peters, R.
Biochemical characterization of the castor bean ent-kaurene synthase(-like) family supports quantum chemical view of diterpene cyclization
Phytochemistry
103
13
2014
Ricinus communis (B9SIL7), Ricinus communis
brenda
Zhan, X.; Bach, S.S.; Hansen, N.L.; Lunde, C.; Simonsen, H.T.
Additional diterpenes from Physcomitrella patens synthesized by copalyl diphosphate/kaurene synthase (PpCPS/KS)
Plant Physiol. Biochem.
96
110-114
2015
Physcomitrium patens (A5A8G0), Physcomitrium patens
brenda
Miyazaki, S.; Toyoshima, H.; Natsume, M.; Nakajima, M.; Kawaide, H.
Blue-light irradiation up-regulates the ent-kaurene synthase gene and affects the avoidance response of protonemal growth in Physcomitrella patens
Planta
240
117-124
2014
Physcomitrium patens (A5A8G0), Physcomitrium patens
brenda
Liu, W.; Feng, X.; Zheng, Y.; Huang, C.H.; Nakano, C.; Hoshino, T.; Bogue, S.; Ko, T.P.; Chen, C.C.; Cui, Y.; Li, J.; Wang, I.; Hsu, S.T.; Oldfield, E.; Guo, R.T.
Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum
Sci. Rep.
4
6214
2014
Bradyrhizobium diazoefficiens (Q45222), Bradyrhizobium diazoefficiens JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 (Q45222)
brenda
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