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Information on EC 5.5.1.13 - ent-copalyl diphosphate synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q38802
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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
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ent-cpp
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ent-kaurenoic
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phytocassanes
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e,e,e-geranylgeranyl
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oscps4
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3-oxidase
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ga-deficient
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labdane-related
- ga1
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ditpss
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oryzalexins
- ga20ox
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syn-copalyl
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ent-kaurene synthase A
-
-
-
-
ent-kaurene synthetase A
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate = ent-copalyl diphosphate
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular lyase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
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)
CAS REGISTRY NUMBER
COMMENTARY
9055-64-5
in Chemical Abstracts not distinguished from EC 4.2.3.19
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
-
-
-
?
additional information
?
-
no activity with (S)-15-aza-14,15-dihydrogeranylgeranyl thiolodiphosphate
-
-
?
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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). KSA_ARATH
802
0
93014
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T421A
the mutant exhibits a 163fold reduction in kcat (KM is increased 2fold)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TPS, genetic organization on the chromosome, genotyping and phylogenetic analysis, detailed overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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