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Information on EC 5.5.1.13 - ent-copalyl diphosphate synthase
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5.5.1.13 ent-copalyl diphosphate synthaseIUBMB Comments
Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase)
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Word Map
- 5.5.1.13
- gibberellin
-
diterpene
-
diterpenoids
-
geranylgeranyl
-
phytohormone
-
phytoalexins
-
ent-cpp
-
ent-kaurenoic
-
phytocassanes
-
e,e,e-geranylgeranyl
-
oscps4
-
3-oxidase
-
ga-deficient
-
labdane-related
- ga1
-
ditpss
-
oryzalexins
- ga20ox
-
syn-copalyl
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ent-copalyl diphosphate synthase, oscps1, ent-cps, ent-kaurene synthase a, oscyc2, gfcps/ks, oscps2ent, ent-kaurene synthetase a, copalyl synthase/kaurene synthase, oscps1ent, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPS
CPS/KS
CPS1
CPS2/Cyc2
-
bifunctional enzyme, acts in the synthesis of oryzalexins A-F and phytocassanes A-E (phytoalexins)
ent-copalyl/ent-kaurene synthase
ent-CPS
ent-kaurene synthase A
-
-
-
-
ent-kaurene synthetase A
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate = ent-copalyl diphosphate
-
-
-
-
geranylgeranyl diphosphate = ent-copalyl diphosphate
reaction mechanism
-
geranylgeranyl diphosphate = ent-copalyl 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
-
geranylgeranyl diphosphate = ent-copalyl 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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular lyase
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ent-copalyl-diphosphate lyase (decyclizing)
Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase)
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CAS REGISTRY NUMBER
COMMENTARY
9055-64-5
in Chemical Abstracts not distinguished from EC 4.2.3.19
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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
(E,E,E)-geranylgeranyl diphosphate
ent-copalyl diphosphate
-
-
-
?
copalyl diphosphate
ent-16-alpha-hydroxy-kaurene + ent-kaurene + diphosphate
-
bifunctional copalyl diphosphate synthase/ent-kaurene synthase
86% and 14%, resp.
-
?
copalyl diphosphate
ent-kaurene + diphosphate
bifunctional enzyme
-
?
copalyl diphosphate
ent-kaurene + diphosphate
bifunctional enzyme
-
?
copalyl diphosphate
ent-kaurene + diphosphate
bifunctional enzyme
-
?
geranylgeranyl diphosphate
copalyl diphosphate
gibberellin biosynthesis
-
?
geranylgeranyl diphosphate
copalyl diphosphate
-
gibberellin biosynthesis
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
-
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
-
the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCPS1 participates in biosynthesis of gibberelins
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCPS1ent normally operates in biosynthesis of gibberellin
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCPS2ent is involved in secondary metabolism producing defensive phytochemicals. OsCPS2ent mRNA is specifically induced in leaves prior to production of the corresponding phytoalexins. The transcriptional control of OsCPS2ent seems to be an important means of regulating defensive phytochemical biosynthesis
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCyc2 is possibly involved in phytoalexin biosynthesis
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
-
the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
transcript levels of the An2 gene encoding copalyl diphosphate synthase are strongly up-regulated by attack by Fusarium graminearum
-
-
?
geranylgeranyl diphosphate
ent-kaurene + ?
-
-
gives ent-kaurene + an unidentified compound
?
additional information
?
-
no activity with (S)-15-aza-14,15-dihydrogeranylgeranyl thiolodiphosphate
-
-
?
additional information
?
-
-
the bifunctional ent-kaurene synthase JsCPS/KS catalyzes the cyclization reaction of geranylgeranyl diphosphate to ent-copalyl diphosohate to produce ent-kaurene, but not 16alpha-hydroxy-ent-kaurane
-
-
?
additional information
?
-
-
the bifunctional ent-kaurene synthase PpCPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
-
?
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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
(E,E,E)-geranylgeranyl diphosphate
ent-copalyl diphosphate
-
-
-
?
copalyl diphosphate
ent-kaurene + diphosphate
bifunctional enzyme
-
?
geranylgeranyl diphosphate
copalyl diphosphate
gibberellin biosynthesis
-
?
geranylgeranyl diphosphate
copalyl diphosphate
-
gibberellin biosynthesis
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCPS1 participates in biosynthesis of gibberelins
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCPS1ent normally operates in biosynthesis of gibberellin
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCPS2ent is involved in secondary metabolism producing defensive phytochemicals. OsCPS2ent mRNA is specifically induced in leaves prior to production of the corresponding phytoalexins. The transcriptional control of OsCPS2ent seems to be an important means of regulating defensive phytochemical biosynthesis
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
OsCyc2 is possibly involved in phytoalexin biosynthesis
-
-
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
transcript levels of the An2 gene encoding copalyl diphosphate synthase are strongly up-regulated by attack by Fusarium graminearum
-
-
?
additional information
?
-
-
the bifunctional ent-kaurene synthase JsCPS/KS catalyzes the cyclization reaction of geranylgeranyl diphosphate to ent-copalyl diphosohate to produce ent-kaurene, but not 16alpha-hydroxy-ent-kaurane
-
-
?
additional information
?
-
-
the bifunctional ent-kaurene synthase PpCPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
or Zn2+, Mg2+, required. Activation in decreasing order: Mg2+, Zn2+, Co2+
Mg2+
Zn2+
-
or Mg2+, Co2+, required. Activation in decreasing order: Mg2+, Zn2+, Co2+
Mg2+
-
or Zn2+, Co2+, required. Activation in decreasing order: Mg2+, Zn2+, Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-isopropyl-4'-(trimethylammonium chloride)-5'-methylphenyl-piperidine-1-carboxylate
AMO-1618, a quaternary ammonium salt, leads to total enzyme inhibition at 0.001 mM
5-isopropyl-N,N,N,2-tetramethyl-4-[(1-piperidinylcarbonyl)oxy]anilinium chloride
-
CPS1 activity exhibits approximately 70% inhibition by 0.1 mM Amo-1618, whereas the OsCPS2/OsCyc2 activity exhibits approximately 10% inhibition
AMO-1618
-
i.e. 2'-isopropyl-4'-(trimethylammoniumchloride)-5'-methylphenylpiperidine-1-carboxylate
geranylgeranyl diphosphate
-
CPS1 but not CPS2/Cyc2 is inhibited by 0.05-0.06 mM geranylgeranyl diphosphate, CPS1 shows significant substrate inhibition in the presence of more than 0.05 mM geranylgeranyl diphosphate
additional information
-
inhibitory effects on partially purified enzyme of 14 quaternary ammonium iodides at 3 different concentrations are reported
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Nighttime Sugar Starvation Orchestrates Gibberellin Biosynthesis and Plant Growth in Arabidopsis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme N425H, at pH 7.8 and 22°C
0.0017
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme E211A, at pH 7.8 and 22°C
0.0018
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme N425A, at pH 7.8 and 22°C
0.002
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme R340A, at pH 7.8 and 22°C
0.0029
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme D503A, at pH 7.8 and 22°C
0.003
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme T421S, at pH 7.8 and 22°C
0.003
(E,E,E)-geranylgeranyl diphosphate
wild type enzyme, at pH 7.8 and 22°C
0.006
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme T421A, at pH 7.8 and 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme R340A, at pH 7.8 and 22°C
0.0019
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme E211A, at pH 7.8 and 22°C
0.006
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme T421A, at pH 7.8 and 22°C
0.012
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme N425H, at pH 7.8 and 22°C
0.071
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme N425A, at pH 7.8 and 22°C
0.13
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme D503A, at pH 7.8 and 22°C
0.3
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme T421S, at pH 7.8 and 22°C
0.9
(E,E,E)-geranylgeranyl diphosphate
wild type enzyme, at pH 7.8 and 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme R340A, at pH 7.8 and 22°C
1
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme T421A, at pH 7.8 and 22°C
1.1
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme E211A, at pH 7.8 and 22°C
20
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme N425H, at pH 7.8 and 22°C
40
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme N425A, at pH 7.8 and 22°C
45
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme D503A, at pH 7.8 and 22°C
100
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme T421S, at pH 7.8 and 22°C
300
(E,E,E)-geranylgeranyl diphosphate
wild type enzyme, at pH 7.8 and 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activity per mg of protein for different plant organs
additional information
-
specific activity per mg of protein for different plant organs
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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 copalyl diphosphate synthase/ent-kaurene synthase
-
-
brenda
bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
OsCPS2ent mRNA is specifically induced in leaves prior to production of the corresponding phytoalexins
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
evolution
-
TPS genes in both gymnosperms and angiosperms are likely derived from a duplication of an ancestral gene encoding a bifunctional kaurene synthase, TPS family size and comparison of physiological functions of TPS enzymes in different organisms, overview. The genomes of some model angiosperms and gymnosperms contain 40-152 TPS genes, not all of them functional and most of the functional ones having lost activity in either the CPS- or KS-type domains. TPS genes are generally divided into seven clades, with some plant lineages having a majority of their TPS genes in one or two clades, indicating lineage-specific expansion of specific types of genes. Evolutionary plasticity is evident in the TPS family, with closely related enzymes differing in their product profiles, subcellular localization, or the in planta substrates they use. Based on the reaction mechanism and products formed, plant TPSs can be classified into two groups: class I and class II, detailed overview
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
metabolism
-
in flowering plants, ent-kaurene is biosynthesized from geranylgeranyl diphosphate by two distinct cyclases, ent-copalyl diphosphate synthase and ent-kaurene synthase
metabolism
-
in flowering plants, entkaurene is biosynthesized from geranylgeranyl diphosphate by two distinct cyclases, ent-copalyl diphosphate synthase and ent-kaurene synthase
physiological function
-
isoforms CPS1 and CPS2 are responsible for the anti-pathogen effects while isoform CPS3 functions in gibberellin biosynthesis
physiological function
-
ent-kaurene, a tetracyclic diterpene hydrocarbon, is the biosynthetic intermediate of the plant hormone gibberellin, and is synthesized from geranylgeranyl diphosphate via ent-copalyl diphosphate. The bifunctional ent-kaurene synthase CPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate. Hydrophobicity and size of the side chain residue at the PpCPS/KS amino acid 710 is responsible for quenching the ent-kauranyl cation by the addition of a water molecule
physiological function
-
the bifunctional ent-kaurene synthase CPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate. Hydrophobicity and size of the side chain residue at the PpCPS/KS amino acid 710 is responsible for quenching the ent-kauranyl cation by the addition of a water molecule
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
physiological function
-
the TPS gene encodes a copalyl synthase/kaurene synthase, CPS/KS, a bifunctional enzyme. Copalyl diphosphate synthase, CPS, and kaurene synthase, KS, convert geranylgeranyl diphosphate first to copalyl diphosphate, then to ent-kaurene, the precursor of all plant gibberellins
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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). CPPS2_MAIZE
825
0
92762
Swiss-Prot
Chloroplast (Reliability: 2)
CPS2_ORYSI
800
0
90006
Swiss-Prot
Mitochondrion (Reliability: 4)
CPS2_ORYSJ
800
0
89937
Swiss-Prot
Mitochondrion (Reliability: 4)
CPS3_ISOER
766
0
87546
Swiss-Prot
Mitochondrion (Reliability: 5)
CPS4_ISORU
796
0
91115
Swiss-Prot
Chloroplast (Reliability: 4)
CPS5_ISORU
664
0
76698
Swiss-Prot
other Location (Reliability: 2)
CPS5_SALMI
793
0
90130
Swiss-Prot
Chloroplast (Reliability: 2)
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)
KSA_ARATH
802
0
93014
Swiss-Prot
Chloroplast (Reliability: 1)
KSA_PEA
801
0
92718
Swiss-Prot
Chloroplast (Reliability: 5)
CPS1_ISOER
710
0
81645
Swiss-Prot
other Location (Reliability: 2)
CPS1_ISOJA
711
0
81749
Swiss-Prot
other Location (Reliability: 2)
CPS1_ORYSJ
867
0
98055
Swiss-Prot
Chloroplast (Reliability: 2)
CPS2_ISOER
794
0
90777
Swiss-Prot
Chloroplast (Reliability: 3)
A0A2I0ADH3_9ASPA
285
0
32799
TrEMBL
other Location (Reliability: 4)
B8MPJ9_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
960
0
107429
TrEMBL
other Location (Reliability: 2)
A0A396GSV5_MEDTR
252
0
29488
TrEMBL
Secretory Pathway (Reliability: 2)
A0A396HGJ0_MEDTR
47
0
5396
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396GXX6_MEDTR
424
0
49323
TrEMBL
Mitochondrion (Reliability: 4)
A0A072TW04_MEDTR
822
0
95144
TrEMBL
Chloroplast (Reliability: 1)
G7KDR7_MEDTR
55
0
6322
TrEMBL
other Location (Reliability: 4)
B9S414_RICCO
800
0
91353
TrEMBL
Chloroplast (Reliability: 1)
A0A2G9HKS9_9LAMI
573
0
66405
TrEMBL
other Location (Reliability: 1)
A0A0B2QJH5_GLYSO
720
0
83032
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396GKS0_MEDTR
102
0
11533
TrEMBL
other Location (Reliability: 2)
A0A1B0YKB9_TRIWF
816
0
94180
TrEMBL
Secretory Pathway (Reliability: 5)
D4III9_HELAN
798
0
91511
TrEMBL
Chloroplast (Reliability: 3)
A0A5B7C8S5_DAVIN
138
0
16392
TrEMBL
other Location (Reliability: 5)
A0A396GVS7_MEDTR
55
0
6468
TrEMBL
other Location (Reliability: 3)
A0A396HND5_MEDTR
42
0
5233
TrEMBL
other Location (Reliability: 5)
X5AIS9_9LAMI
637
0
73515
TrEMBL
other Location (Reliability: 2)
A0A8F6T501_9LAMI
819
0
93372
TrEMBL
Chloroplast (Reliability: 2)
A0A396GUW8_MEDTR
387
0
44338
TrEMBL
Chloroplast (Reliability: 1)
A0A2R4SC20_CAMSI
843
0
96872
TrEMBL
Chloroplast (Reliability: 3)
A0A0B2QF47_GLYSO
815
0
93593
TrEMBL
Chloroplast (Reliability: 2)
A0A2G9HL53_9LAMI
808
0
92316
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6PW10_ROSCH
825
0
93977
TrEMBL
Chloroplast (Reliability: 1)
A0A5C0T860_SALSC
605
0
69372
TrEMBL
other Location (Reliability: 2)
A0A396HQG7_MEDTR
130
0
15157
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6PW04_ROSCH
857
0
98519
TrEMBL
other Location (Reliability: 2)
A0A5B7B435_DAVIN
343
0
40195
TrEMBL
other Location (Reliability: 3)
R9W4U8_9ROSA
799
0
91470
TrEMBL
Mitochondrion (Reliability: 3)
A0A396HEE2_MEDTR
176
0
20626
TrEMBL
other Location (Reliability: 3)
A0A396H482_MEDTR
695
0
81105
TrEMBL
other Location (Reliability: 2)
D2X8G2_PICSI
761
0
87775
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
101000
-
x * 101000, calculated, x * 106000, SDs-PAGE of myc-fusion protein
106000
106000
-
x * 101000, calculated, x * 106000, SDs-PAGE of myc-fusion protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with (S)-15-aza-14,15-dihydrogeranylgeranyl thiolodiphosphate, vapor diffusion method, using 100 mM sodium citrate (pH 5.4), 30% (w/v) polyethylene glycol 400, 200 mM KH2PO4
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T421A
the mutant exhibits a 163fold reduction in kcat (KM is increased 2fold)
A710C
A710F
A710G
A710L
-
the substitution changes the ratio of ent-kaurene and 16alpha-hydroxy-entkaurane produced. The production of ent-kaurene is increased to the same level as that of 16alpha-hydroxyent-kaurane
A710M
A710N
A710S
C717A
-
site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS
additional information
A710C
-
site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
A710F
-
mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product
A710F
-
site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS
A710G
-
site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
A710M
-
mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product
A710M
-
site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS
A710N
-
site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
A710S
-
site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
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
-
Jungermannia subulata JsCPS/KS peptide fragments are replaced by the corresponding Physcomitrella patens PpCPS/KS region. A PCR-amplified Jungermannia subulata JsCPS/KS DNA fragment corresponding to amino acids 574-746 is replaced by Physcomitrella patens PpCPS/KS amino acids 566-740. Four chimeric cyclases, Physcomitrella patens Pp566/Js574-746/Pp740, Pp566/Js574-721/Pp715, Pp627/Js635-721/Pp715, and Pp666/Js674-721/Pp715, have enzymic activity and produce only ent-kaurene from geranylgeranyl diphosphate, like Jungermannia subulata JsCPS/KS. The chimeric cyclase Pp566/Js574-634/Pp628 shows the same activity as wild-type PpCPS/KS, converting geranylgeranyl diphosphate to both ent-kaurene and 16alpha-hydroxy-ent-kaurane. Overview mutant chimeric constructs and enzymatic activity
additional information
-
sequence contains a DVDD motif responsible for copalyl diphosphate synthase activity and a DDYFD motif responsible for ent-kaurene synthase activity. Mutation of DVDD motif to AVAD leads to loss of function, mutation of DDYFD motif to AAYFD results in accumulation of ent-copalyl diphosphate
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
-
Jungermannia subulata JsCPS/KS peptide fragments are replaced by the corresponding Physcomitrella patens PpCPS/KS region. A PCR-amplified Jungermannia subulata JsCPS/KS DNA fragment corresponding to amino acids 574-746 is replaced by Physcomitrella patens PpCPS/KS amino acids 566-740. Four chimeric cyclases, Physcomitrella patens Pp566/Js574-746/Pp740, Pp566/Js574-721/Pp715, Pp627/Js635-721/Pp715, and Pp666/Js674-721/Pp715, have enzymic activity and produce only ent-kaurene from geranylgeranyl diphosphate, like Jungermannia subulata JsCPS/KS. The chimeric cyclase Pp566/Js574-634/Pp628 shows the same activity as wild-type PpCPS/KS, converting geranylgeranyl diphosphate to both ent-kaurene and 16alpha-hydroxy-ent-kaurane. Overview mutant chimeric constructs and enzymatic activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
activity is fully retained after incubating at 30°C in 0.05 M Tris-HCl at pH 7.0 for 1 h
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-mercaptoethanol
-
5 mM 2-mercaptoethanol is required for full enzymatic activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap nickel-affinity column chromatography
partial, using ammonium sulfate fractionation
partial, using ammonium sulfate fractionation, column chromatography on Sephadex G25
recombinant enzyme, using Sepharose 4B glutathione affinity resin and SDS PAGE electrophoresis
using ammonium sulfate fractionation, Sephadex A-50 chromatography and PAGE electrophoresis
-
partial, using ammonium sulfate fractionation, column chromatography on Sephadex G25
-
partial, using ammonium sulfate fractionation, column chromatography on Sephadex G25
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli C41 cells
expression as myc-fusion protein using Spodoptera frugiperda 21 insect cells. Sequence contains a DVDD motif responsible for copalyl diphosphate synthase activity and a DDYFD motif responsible for ent-kaurene synthase activity
-
expression in Escherichia coli of a recombinant GST fused enzyme
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
expression in Escherichia coli of a recombinant GST fused enzyme
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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)
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.
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.; 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
-
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
Cucurbita maxima, Phaeosphaeria sp. (O13284)
brenda
Ait-Ali, T.; Swain, S.M.; Reid, J.B.; Sun, T.; Kamiya, Y.
The LS locus of pea encodes the gibberellin biosynthesis enzyme ent-kaurene synthase A
Plant J.
11
443-454
1997
Pisum sativum
brenda
Otsuka, M.; Kenmoku, H.; Ogawa, M.; Okada, K.; Mitsuhashi, W.; Sassa, T.; Kamiya, Y.; Toyomasu, T.; Yamaguchi, S.
Emission of ent-kaurene, a diterpenoid hydrocarbon precursor for gibberellins, into the headspace from plants
Plant Cell Physiol.
45
1129-1138
2004
Fusarium fujikuroi
brenda
Otomo, K.; Kenmoku, H.; Oikawa, H.; Konig, W.A.; Toshima, H.; Mitsuhashi, W.; Yamane, H.; Sassa, T.; Toyomasu, T.
Biological functions of ent- and syn-copalyl diphosphate synthases in rice: key enzymes for the branch point of gibberellin and phytoalexin biosynthesis
Plant J.
39
886-893
2004
Oryza sativa, Oryza sativa (Q6Z5I0)
brenda
Harris, L.J.; Saparno, A.; Johnston, A.; Prisic, S.; Xu, M.; Allard, S.; Kathiresan, A.; Ouellet, T.; Peters, R.J.
The maize An2 gene is induced by Fusarium attack and encodes an ent-copalyl diphosphate synthase
Plant Mol. Biol.
59
881-894
2005
Zea mays
brenda
Prisic, S.; Xu, M.; Wilderman, P.R.; Peters, R.J.
Rice contains two disparate ent-copalyl diphosphate synthases with distinct metabolic functions
Plant Physiol.
136
4228-4236
2004
Oryza sativa, Oryza sativa (Q5MQ85)
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
brenda
Ikeda, C.; Hayashi, Y.; Itoh, N.; Seto, H.; Dairi, T.
Functional analysis of eubacterial ent-copalyl diphosphate synthase and pimara-9(11),15-diene synthase with unique primary sequences
J. Biochem.
141
37-45
2007
Streptomyces sp., Streptomyces sp. KO-3988
brenda
Sawada, Y.; Katsumata, T.; Kitamura, J.; Kawaide, H.; Nakajima, M.; Asami, T.; Nakaminami, K.; Kurahashi, T.; Mitsuhashi, W.; Inoue, Y.; Toyomasu, T.
Germination of photoblastic lettuce seeds is regulated via the control of endogenous physiologically active gibberellin content, rather than of gibberellin responsiveness
J. Exp. Bot.
59
3383-3393
2008
Lactuca sativa (Q9FXV9)
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 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
Toyomasu, T.; Kagahara, T.; Hirose, Y.; Usui, M.; Abe, S.; Okada, K.; Koga, J.; Mitsuhashi, W.; Yamane, H.
Cloning and characterization of cDNAs encoding ent-copalyl diphosphate synthases in wheat: Insight into the evolution of rice phytoalexin biosynthetic genes
Biosci. Biotechnol. Biochem.
73
772-775
2009
Triticum aestivum
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
Picea glauca (D2X8G0), Picea sitchensis (D2X8G2)
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
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
Physcomitrium patens, Liochlaena subulata
brenda
Chen, F.; Tholl, D.; Bohlmann, J.; Pichersky, E.
The family of terpene synthases in plants: A mid-size family of genes for specialized metabolism that is highly diversified throughout the kingdom
Plant J.
66
212-229
2011
Abies grandis, Arabidopsis thaliana, Oryza sativa, Physcomitrium patens, Picea abies, Picea glauca, Populus trichocarpa, Sorghum bicolor, Vitis vinifera, Picea sitchensis, Selaginella moellendorffii, Picea engelmannii x Picea glauca
brenda
Koeksal, M.; Potter, K.; Peters, R.J.; Christianson, D.W.
1.55 A-resolution structure of ent-copalyl diphosphate synthase and exploration of general acid function by site-directed mutagenesis
Biochim. Biophys. Acta
1840
184-190
2014
Arabidopsis thaliana (Q38802)
brenda
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Release 2023.1 (January 2023)
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