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Information on EC 5.5.1.13 - ent-copalyl diphosphate synthase
for references in articles please use BRENDA:EC5.5.1.13
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EC Tree 5 Isomerases
5.5 Intramolecular lyases
5.5.1 Intramolecular lyases (only sub-subclass identified to date)
5.5.1.13 ent-copalyl diphosphate synthase
IUBMB Comments
Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase)
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 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
showSynonyms
ent-copalyl diphosphate synthase, oscps1, ent-cps, ent-kaurene synthase a, oscyc2, gfcps/ks, oscps2ent, oscps1ent, ent-kaurene synthetase a, copalyl synthase/kaurene synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPS
CPS/KS
CPS1
CPS2
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
-
-
-
-
KSL12
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate = ent-copalyl diphosphate
-
-
-
-
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
-
geranylgeranyl diphosphate = ent-copalyl diphosphate
reaction mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular lyase
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
diterpene phytoalexins precursors biosynthesis, dolabralexins biosynthesis, ent-kaurene biosynthesis I, kauralexin biosynthesis, platensimycin biosynthesis
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E,E,E)-geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-16-alpha-hydroxy-kaurene + ent-kaurene + diphosphate
-
Substrates: bifunctional copalyl diphosphate synthase/ent-kaurene synthase
Products: 86% and 14%, resp.
Products: 86% and 14%, resp.
?
geranylgeranyl diphosphate
ent-kaurene + diphosphate
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
-
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
-
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: bifunctional enzyme
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
-
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: bifunctional enzyme
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
-
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
Substrates: gibberellin biosynthesis
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
-
Substrates: gibberellin biosynthesis
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
Products: 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
Substrates: OsCPS1ent normally operates in biosynthesis of gibberellin
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: 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
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: OsCPS1 participates in biosynthesis of gibberelins
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: OsCyc2 is possibly involved in phytoalexin biosynthesis
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
Products: 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
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: transcript levels of the An2 gene encoding copalyl diphosphate synthase are strongly up-regulated by attack by Fusarium graminearum
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-kaurene + ?
-
Substrates: -
Products: gives ent-kaurene + an unidentified compound
Products: gives ent-kaurene + an unidentified compound
?
geranylgeranyl diphosphate
geranyllinalool + diphosphate
-
Substrates: the reaction is catalyzed by isoform KSL12
Products: -
Products: -
?
geranylgeranyl diphosphate
geranyllinalool + diphosphate
-
Substrates: the reaction is catalyzed by isoform KSL12
Products: -
Products: -
?
geranylgeranyl diphosphate
geranyllinalool + diphosphate
-
Substrates: the reaction is catalyzed by isoform KSL12
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with (S)-15-aza-14,15-dihydrogeranylgeranyl thiolodiphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional ent-kaurene synthase PpCPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E,E,E)-geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
copalyl diphosphate
ent-kaurene + diphosphate
Substrates: bifunctional enzyme
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-kaurene + diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
Substrates: gibberellin biosynthesis
Products: -
Products: -
?
geranylgeranyl diphosphate
copalyl diphosphate
-
Substrates: gibberellin biosynthesis
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: OsCPS1ent normally operates in biosynthesis of gibberellin
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: 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
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: OsCPS1 participates in biosynthesis of gibberelins
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: OsCyc2 is possibly involved in phytoalexin biosynthesis
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl diphosphate
ent-copalyl diphosphate
-
Substrates: transcript levels of the An2 gene encoding copalyl diphosphate synthase are strongly up-regulated by attack by Fusarium graminearum
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional ent-kaurene synthase PpCPS/KS produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate
Products: -
Products: -
?
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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
wild type enzyme, at pH 7.8 and 22°C
0.003
(E,E,E)-geranylgeranyl diphosphate
mutant enzyme T421S, at pH 7.8 and 22°C
0.006
(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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TEMPERATURE RANGE
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, entkaurene is biosynthesized from geranylgeranyl diphosphate by two distinct cyclases, ent-copalyl diphosphate synthase and ent-kaurene synthase
metabolism
-
in flowering plants, ent-kaurene 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
-
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 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
-
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 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). CPS4_ISORU
796
0
91115
Swiss-Prot
Secretory Pathway (Reliability: 4)
PBCA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
979
0
110118
Swiss-Prot
-
CPSKS_PHASA
Phaeosphaeria sp. (strain L487)
946
0
105724
Swiss-Prot
Secretory Pathway (Reliability: 1)
ECDPS_STREO
Streptomyces sp. (strain KO-3988)
511
0
54768
Swiss-Prot
other Location (Reliability: 1)
GA6_GIBF5
Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831)
952
0
106762
Swiss-Prot
-
A0A0D9VHD3_9ORYZ
781
0
88170
TrEMBL
other Location (Reliability: 1)
A0A0E0H9N2_ORYNI
848
0
95736
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0E0NGP2_ORYRU
800
0
89994
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1B4X957_ORYBR
771
0
87994
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1Z5S7J8_SORBI
723
0
83441
TrEMBL
other Location (Reliability: 1)
A0A6G1D0R7_9ORYZ
786
0
88659
TrEMBL
-
A0A6G1F9S6_9ORYZ
838
0
96003
TrEMBL
-
A0A6G1F9U9_9ORYZ
833
0
95259
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6G1FA21_9ORYZ
852
0
97511
TrEMBL
-
A0A6G1F9U4_9ORYZ
844
0
96614
TrEMBL
-
A0A6G1FA51_9ORYZ
830
0
95106
TrEMBL
-
A0A6G1F9X1_9ORYZ
819
0
93750
TrEMBL
-
A0A804LMB4_MAIZE
833
0
93418
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8F6T501_9LAMI
819
0
93372
TrEMBL
other Location (Reliability: 5)
B8AFL6_ORYSI
864
0
97568
TrEMBL
Secretory Pathway (Reliability: 1)
A0A023VSF1_STRPT
533
0
55498
TrEMBL
other Location (Reliability: 3)
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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
D336L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D336L/D377L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D336L/G422L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D336L/K778F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D336L/S597W
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D377A
the mutant shows decreased catalytic function compared to the wild type enzyme
D377K
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D377L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D377L/G422L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D377L/K778F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D377L/S597W
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
D379A
the mutant shows decreased catalytic function compared to the wild type enzyme
D380A
the mutant shows decreased catalytic function compared to the wild type enzyme
G422L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
G422L/K778F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
G422L/S597W
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
G422M
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
H331A
the mutant shows decreased catalytic function compared to the wild type enzyme
H331R
the mutant shows decreased catalytic function compared to the wild type enzyme
H391L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
H391M
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
H793F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
H793L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
H793M
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
K778F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
K778W
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
S597W
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
S597W/K778F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
T114F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
T114F/D336L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
T114F/D377L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
T114F/G422L
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
T114F/K778F
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
T114F/S597W
the mutant exhibits improved affinity for geranylgeranyl diphosphate compared to the wild type enzyme
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
G347P
the mutant shows about 270% activity at 40°C and increased melting temperature compared to the wild type enzyme
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 BL21(DE3) cells
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcript level of isoform KSL12 in UV-irradiated leaf sheath is higher than that in mock control sample
the transcript level of isoform KSL12 in UV-irradiated leaf sheath is higher than that in mock control sample
-
the transcript level of isoform KSL12 in UV-irradiated leaf sheath is higher than that in mock control sample
-
the transcript level of isoform KSL12 in UV-irradiated leaf sheath is higher than that in mock control sample
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawaide, H.; Imai, R.; Sassa, T.; Kamiya, Y.
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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
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Fusarium fujikuroi (Q9UVY5)
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Marah macrocarpa
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Shen-Miller, J.; West, C.A.
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Phytochemistry
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Helianthus annuus, Marah macrocarpa
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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
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Cucurbita maxima, Lathyrus oleraceus, Triticum aestivum
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Saito, T.; Yamane, H.; Sakurai, A.; Murofushi, N.; Takahashi, N.; Kamiya, Y.
Inhibition of ent-kaurene synthase by quaternary ammonium growth retardants
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Cucurbita maxima
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Aach, H.; Bode, H.; Robinson, D.G.; Graebe, J.E.
ent-Kaurene synthase is located in proplastids of meristematic shoot tissues
Planta
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Lathyrus oleraceus, Triticum aestivum
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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
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Cucurbita maxima, Phaeosphaeria sp. (O13284)
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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.
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Lathyrus oleraceus
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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
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Fusarium fujikuroi
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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.
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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
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Zea mays
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Prisic, S.; Xu, M.; Wilderman, P.R.; Peters, R.J.
Rice contains two disparate ent-copalyl diphosphate synthases with distinct metabolic functions
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Oryza sativa, Oryza sativa (Q5MQ85)
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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
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Physcomitrium patens
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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
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Streptomyces sp., Streptomyces sp. KO-3988
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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
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Lactuca sativa (Q9FXV9)
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Boemke, C.; Rojas, M.C.; Gong, F.; Hedden, P.; Tudzynski, B.
Isolation and characterization of the gibberellin biosynthetic gene cluster in Sphaceloma manihoticola
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Sphaceloma manihoticola (B5DBY7), Sphaceloma manihoticola Lu949 (B5DBY7)
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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
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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
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Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
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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
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Triticum aestivum
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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
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Picea sitchensis (D2X8G2), Picea glauca (D2X8G0)
brenda
Anterola, A.; Shanle, E.; Mansouri, K.; Schuette, S.; Renzaglia, K.
Gibberellin precursor is involved in spore germination in the moss Physcomitrella patens
Planta
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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
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Physcomitrium patens, Liochlaena subulata
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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
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Populus trichocarpa, Oryza sativa, Sorghum bicolor, Vitis vinifera, Abies grandis, Physcomitrium patens, Selaginella moellendorffii, Picea abies, Picea glauca, Picea sitchensis, Picea engelmannii x Picea glauca, Arabidopsis thaliana
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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
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184-190
2014
Arabidopsis thaliana (Q38802)
brenda
Mao, L.; Jin, B.; Chen, L.; Tian, M.; Ma, R.; Yin, B.; Zhang, H.; Guo, J.; Tang, J.; Chen, T.; Lai, C.; Cui, G.; Huang, L.
Functional identification of the terpene synthase family involved in diterpenoid alkaloids biosynthesis in Aconitum carmichaelii
Acta Pharm. Sin. B
11
3310-3321
2021
Aconitum carmichaelii (A0A8E8TY42), Aconitum carmichaelii (A0A8E8TYD4), Aconitum carmichaelii (A0A8E8TY93), Aconitum carmichaelii (A0A8E8TXV6)
brenda
Itoh, A.; Nakazato, S.; Wakabayashi, H.; Hamano, A.; Shenton, M.R.; Miyamoto, K.; Mitsuhashi, W.; Okada, K.; Toyomasu, T.
Functional kaurene-synthase-like diterpene synthases lacking a gamma domain are widely present in Oryza and related species
Biosci. Biotechnol. Biochem.
85
1945-1952
2021
Oryza sativa Japonica Group (Q6ET36), Oryza sativa Japonica Group (Q6Z5I0), Leersia tisserantii, Oryza meyeriana var. granulata, Leersia perrieri
brenda
Derkx, A.; Baumann, U.; Cheong, J.; Mrva, K.; Sharma, N.; Pallotta, M.; Mares, D.
A major locus on wheat chromosome 7B associated with late-maturity alpha-amylase encodes a putative ent-copalyl diphosphate synthase
Front. Plant Sci.
12
637685
2021
Triticum aestivum
brenda
Szymczyk, P.; Szymanska, G.; Lipert, A.; Weremczuk-Jezyna, I.; Kochan, E.
Computer-aided saturation mutagenesis of Arabidopsis thaliana ent-copalyl diphosphate synthase
Interdiscip. Sci.
12
32-43
2020
Arabidopsis thaliana (Q38802)
brenda
Yang, M.; Liu, G.; Yamamura, Y.; Chen, F.; Fu, J.
Divergent evolution of the diterpene biosynthesis pathway in tea plants (Camellia sinensis) caused by single amino acid variation of ent-kaurene synthase
J. Agric. Food Chem.
68
9930-9939
2020
Camellia sinensis (A0A2R4SC20)
brenda
Hueting, D.A.; Vanga, S.R.; Syren, P.O.
Thermoadaptation in an ancestral diterpene cyclase by altered loop stability
J. Phys. Chem. B
126
3809-3821
2022
Streptomyces platensis (A0A023VSF1)
brenda
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