Information on EC 4.2.3.127 - beta-copaene synthase

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The expected taxonomic range for this enzyme is: Coprinopsis cinerea

EC NUMBER
COMMENTARY hide
4.2.3.127
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RECOMMENDED NAME
GeneOntology No.
beta-copaene synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, bet6a-copaene-forming)
Isolated from the fungus Coprinus cinereus. The enzyme also forms (+)-delta-cadinene, beta-cubebene, (+)-sativene and traces of several other sequiterpenoids [1-3]. beta-Copaene is formed in the presence of Mg2+ but not Mn2+ [2]. See EC 4.2.3.13, (+)-delta-cadinene synthase, EC 4.2.3.128, beta-cubebene synthase, and EC 4.2.3.129, (+)-sativene synthase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
beta-copaene + diphosphate
show the reaction diagram
(E)-geranyl diphosphate
?
show the reaction diagram
-
the enzyme accepts (E)-geranyl diphosphate as a substrate, but the catalytic efficiency with the shorter prenyl-diphosphate substrate is lower compared to their longer farnesyl diphosphate substrate
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
beta-copaene + diphosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.0707
(2E,6E)-farnesyl diphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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mutant enzymes N239L, H235P, and K233I
8
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wild-type enzyme
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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lowering the reaction temperature from 25C to 4C increases the selectivity of Cop4 for (-)-germacrene D. Increasing the reaction temperature to 37C has the opposite effect and decreases the fidelity of Cop4. At this temperature Cop4 generates a relative larger fraction of products beta-cubebene, sativene delta-cadinene, and beta-copaene that are derived from a cadinyl cation intermediate
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant Cop4 in Escherichia coli strain JM109
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gene cop4, phylogenetic analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H235P
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site-directed mutagenesis, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4
K233I
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site-directed mutagenesis, the mutant shows a highly altered product profile compared to the wild-type enzyme with decrease in beta-copaene amounts. Cop4 loop mutant K2331 also becomes more selective for ()-germacrene D under acidic or basic reaction conditions, although less so than the wild-type enzyme
N238L
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site-directed mutagenesis, the mutant shows a slightly altered product profile compared to the wild-type enzyme with increase in beta-copaene amounts
N239L
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site-directed mutagenesis, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4
T236L
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site-directed mutagenesis, the mutant shows a slightly altered product profile compared to the wild-type enzyme with increase in beta-copaene amounts