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Information on EC 5.5.1.12 - copalyl diphosphate synthase and Organism(s) Selaginella moellendorffii and UniProt Accession G9MAN7

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EC Tree
IUBMB Comments
In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. In other plants this activity is often a part of a bifunctional enzyme. For example, in Selaginella moellendorffii this activity is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.131, miltiradiene synthase, while in the tree Abies grandis (grand fir) it is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.18, abietadiene synthase.
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This record set is specific for:
Selaginella moellendorffii
UNIPROT: G9MAN7
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Word Map
The taxonomic range for the selected organisms is: Selaginella moellendorffii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
copalyl diphosphate synthase, abietadiene synthase, smcps, smcps1, bifunctional diterpene cyclase, class ii diterpene synthase, class ii ditps, (+)-copalyl diphosphate synthase, cpp synthase, rocps1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bifunctional diterpene cyclase
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(-)-abietadiene synthase
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abietadiene cyclase
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cyclase, abietadiene
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular cyclization
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(+)-copalyl-diphosphate lyase (decyclizing)
In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. In other plants this activity is often a part of a bifunctional enzyme. For example, in Selaginella moellendorffii this activity is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.131, miltiradiene synthase, while in the tree Abies grandis (grand fir) it is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.18, abietadiene synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
157972-08-2
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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
(+)-copalyl diphosphate
show the reaction diagram
BDTC-like enzyme, miltiradiene synthase converts geranylgeranyl diphosphate to a diterpene hydrocarbon product with a molecular mass of 272 Da. Mutation in the type-B active motif of BDTC-like enzyme miltiradiene synthase, D611G/D612G, abolishes the cyclase activity, whereas (+)-copalyl diphosphate, the reaction intermediate from the conversion of geranylgeranyl diphosphate to the hydrocarbon product, rescues the cyclase activity of the mutant to form a diterpene hydrocarbon. Another mutant lacking type-A activity, D391G/D392G, accumulates copalyl diphosphate as the reaction intermediate
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additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
bifunctional diterpene cyclases are involved in hormone and defense compound biosyntheses in bryophytes and gymnosperms, respectively
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPS4_SELML
867
0
99915
Swiss-Prot
Chloroplast (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D391G/D392G
site-directed mutagenesis of DIDD motif residues, the mutant lacks type-B activity
D611G/D612G
site-directed mutagenesis of DDLMD motif residues, the mutant lacks type-A cyclase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sugai, Y.; Ueno, Y.; Hayashi, K.; Oogami, S.; Toyomasu, T.; Matsumoto, S.; Natsume, M.; Nozaki, H.; Kawaide, H.
Enzymatic (13)C labeling and multidimensional NMR analysis of miltiradiene synthesized by bifunctional diterpene cyclase in Selaginella moellendorffii
J. Biol. Chem.
286
42840-42847
2011
Selaginella moellendorffii (G9MAN7), Selaginella moellendorffii
Manually annotated by BRENDA team