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Information on EC 5.5.1.14 - syn-copalyl-diphosphate synthase and Organism(s) Oryza sativa and UniProt Accession Q6E7D7

for references in articles please use BRENDA:EC5.5.1.14
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EC Tree
IUBMB Comments
Requires a divalent metal ion, preferably Mg2+, for activity. This class II terpene synthase produces syn-copalyl diphosphate, a precursor of several rice phytoalexins, including oryzalexin S and momilactones A and B. Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation. The enzyme is constitutively expressed in the roots of plants where one of its products, momilactone B, acts as an allelochemical (a molecule released into the environment to suppress the growth of neighbouring plants). In other tissues the enzyme is upregulated by conditions that stimulate the biosynthesis of phytoalexins.
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This record set is specific for:
Oryza sativa
UNIPROT: Q6E7D7
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Word Map
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  • 5.5.1.14
  • diterpene
  • phytoalexins
  • sativa
  • diterpenoids
  • oryzae
  • phytocassanes
  • oscps4
  • momilactones
  • oryzalexins
  • allelopathic
  • labdane-related
  • gibberellins
  • phytohormone
  • ent-cpp
  • geranylgeranyl
  • cyclization
The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
Synonyms
oscyc1, syn-copalyl diphosphate synthase, oscpssyn, syn-cpp synthase, syn-cdp synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
syn-copalyl diphosphate synthase
-
syn-CDP synthase
-
syn-copalyl diphosphate lyase (decyclizing)
-
-
-
-
syn-copalyl diphosphate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate = 9alpha-copalyl diphosphate
show the reaction diagram
in contrast to EC 5.5.1.12 and EC 5.5.1.13, this enzyme produces copalyl diphosphate having the syn conformation
geranylgeranyl diphosphate = 9alpha-copalyl diphosphate
show the reaction diagram
in contrast to EC 5.5.1.12 and EC 5.5.1.13, this enzyme produces copalyl diphosphate having the syn conformation
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular lyase
-
intramolecular lyase
-
SYSTEMATIC NAME
IUBMB Comments
9alpha-copalyl-diphosphate lyase (decyclizing)
Requires a divalent metal ion, preferably Mg2+, for activity. This class II terpene synthase produces syn-copalyl diphosphate, a precursor of several rice phytoalexins, including oryzalexin S and momilactones A and B. Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation. The enzyme is constitutively expressed in the roots of plants where one of its products, momilactone B, acts as an allelochemical (a molecule released into the environment to suppress the growth of neighbouring plants). In other tissues the enzyme is upregulated by conditions that stimulate the biosynthesis of phytoalexins.
CAS REGISTRY NUMBER
COMMENTARY hide
173585-12-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate
syn-copalyl diphosphate
show the reaction diagram
-
precursor of the phytoalexins oryzalexin S, momilactone A, and momilactone B
-
?
geranylgeranyl diphosphate
syn-copalyl diphosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate
syn-copalyl diphosphate
show the reaction diagram
-
precursor of the phytoalexins oryzalexin S, momilactone A, and momilactone B
-
?
geranylgeranyl diphosphate
syn-copalyl diphosphate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
indica cultivar-group
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
deduced from the existence of a transit peptide sequence
Manually annotated by BRENDA team
deduced from the existence of a transit peptide sequence
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the OsCPS4 knockdown mutant cps4-tos is more susceptible to rice blast fungus than the wild-type, possibly due to lower levels of momilactones and oryzalexin S in the mutant
metabolism
-
the syn-copalyl diphosphate synthase is responsible for phytoalexins momilactones and oryzalexin S biosynthesis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
generation of an OsCPS4 knockdown mutant, cps4-tos. Because Tos17 is inserted into the third intron of OsCPS4, the mature OsCPS4 mRNA is detected in the cps4-tos mutant as well as the wild type, screening Tos17 mutant lines using PCR. Mature OsCPS4 transcript levels in the cps4-tos mutant are about one sixth those in the wild-type. The cps4-tos mutant is more susceptible to rice blast fungus than the wild-type, possibly due to lower levels of momilactones and oryzalexin S in the mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hydroxyapatite chromatography, only partially purified
affinity chromatography using Glutathione Sepharose B
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the full-length preprotein including the transit peptid in Escherichia coli, protein alone and as a C-terminal fusion to glutathione-S-transferase. Additionally, a partial cDNA sequence resembling the mature native protein was expressed alone as a potential pseudomature protein
expression of the full-length protein as a fusion protein with glutathione-S-transferase at the N-terminus in Escherichia coli XL1-Blue
genotyping of the Tos17 insertion mutant
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q0JF02), Oryza sativa
Manually annotated by BRENDA team
Xu, M.; Hillwig, M.L.; Prisic, S.; Coates, R.M.; Peters, R.J.
Functional identification of rice syn-copalyl diphosphate synthase and its role in initiating biosynthesis of diterpenoid phytoalexin/allelopathic natural products
Plant J.
39
309-318
2004
Oryza sativa (Q6E7D7), Oryza sativa
Manually annotated by BRENDA team
Toyomasu, T.; Usui, M.; Sugawara, C.; Otomo, K.; Hirose, Y.; Miyao, A.; Hirochika, H.; Okada, K.; Shimizu, T.; Koga, J.; Hasegawa, M.; Chuba, M.; Kawana, Y.; Kuroda, M.; Minami, E.; Mitsuhashi, W.; Yamane, H.
Reverse-genetic approach to verify physiological roles of rice phytoalexins: characterization of a knockdown mutant of OsCPS4 phytoalexin biosynthetic gene in rice
Physiol. Plant.
150
55-62
2014
Oryza sativa
Manually annotated by BRENDA team