Information on EC 4.2.3.15 - myrcene synthase

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The expected taxonomic range for this enzyme is: Eukaryota

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
4.2.3.15
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SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
myrcene synthase
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SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = myrcene + diphosphate
show the reaction diagram
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-
-
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SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination, C-O bond cleavage
-
-
-
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SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ipsdienol biosynthesis
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monoterpene biosynthesis
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oleoresin monoterpene volatiles biosynthesis
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Monoterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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SplaateSystematic_Name,Commentary_IUBMB
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase (myrcene-forming)
A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
myrcene synthase
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-
myrcene/(E)-beta-ocimene synthase
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SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
197462-59-2
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SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
grand fir
Uniprot
Manually annotated by BRENDA team
; the tandem arginine motif RRX8W is conserved in the deduced protein of TPS10; bifunctional myrcene/(E)-beta-ocimene synthase
SwissProt
Manually annotated by BRENDA team
bifunctional enzyme: geranyldiphosphate synthase/myrcene synthase
SwissProt
Manually annotated by BRENDA team
marine red alga
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-
Manually annotated by BRENDA team
SplaateGeneral_Information, Organism, Commentary, Literature
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
-
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
-
-
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
-
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
-
-
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
56% of total hydrocarbon product
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
products of Arabidopsis thaliana TPS10 are 56% beta-myrcene, 20% (E)-beta-ocimene, and less than 5% each of (+)-limonene, (-)-limonene, 2-carene, and tricyclene and an unknown monoterpene
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
induced by stem wounding, enhances resistance to insects
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?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
the acyclic monoterpene myrcene is required for the production of the major aggregation pheromone component, ipsdienol, bifunctional enzyme: geranyldiphosphate synthase (EC 2.5.1.1)/myrcene synthase (EC 4.2.3.15). When the recombinant enzyme is incubated with dimethylallyl diphosphate and isopentenyl diphosphate as cosubstrates, the level of geranyl diphosphate formed is approximately tenfold higher than the level of myrcene formed. The data suggest that geranyl diphosphate is a free intermediate in myrcene production
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?
geranyl diphosphate
(E)-beta-ocimene
show the reaction diagram
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20% of total hydrocarbon product
?
geranyl diphosphate
(+)-limonene
show the reaction diagram
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less than 5% of total hydrocarbon product
?
geranyl diphosphate
(-)-limonene
show the reaction diagram
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less than 5% of total hydrocarbon product
?
geranyl diphosphate
2-carene
show the reaction diagram
-
less than 5% of total hydrocarbon product
?
geranyl diphosphate
tricyclene
show the reaction diagram
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less than 5% of total hydrocarbon product
?
geranyl diphosphate
myrcene + sabinene + linalool + limonene + diphosphate
show the reaction diagram
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-
formation of 53.8% myrcene, 20.9% sabinene, 19.8% linalool and 5.5% limonene
?
neryl diphosphate
limonene
show the reaction diagram
-
-
-
?
linalyl diphosphate
acyclic and cyclic monoterpenes
show the reaction diagram
-
-
-
?
additional information
?
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terpenes produced from the wild-type and mutant enzymes are identical, showing low levels of beta-myrcene from AcTPS2-K514A
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SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
-
-
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
Q9ZUH4
-
-
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
O24474
induced by stem wounding, enhances resistance to insects
-
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
Q58GE8
the acyclic monoterpene myrcene is required for the production of the major aggregation pheromone component, ipsdienol
-
?
additional information
?
-
-
terpenes produced from the wild-type and mutant enzymes are identical, showing low levels of beta-myrcene from AcTPS2-K514A
-
-
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SplaateCofactor,Organism,Commentary,Literature,Filename
SplaateMetals_Ions,Organism,Commentary, Literature
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
required, optimum concentration of 0.5 M
Mg2+
ineffective
Mg2+
-
required for activity
Mg2+
-
10 mM are included in farnesyl diphosphate activity assay
Mg2+
-
sequence contains conserved sequences R28(R)X8W and D321DXXD encoing putative Mg2+-binding sites
Mn2+
required
additional information
-
wild-type AcTPS2 is significantly more active when KCl is absent from the activity buffer
SplaateInhibitors, Organism, Commentary, Literature,Filename
SplaateActivating_Compound, Organism, Commentary, Literature,Filename
SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
farnesyl diphosphate activity assay
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
farnesyl diphosphate and geranyl diphosphate activity assay
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression correlates well with floral volatile organic compounds emission in scented Alstroemeria genotypes
Manually annotated by BRENDA team
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
SplaateMolecular_Weight, Molecular_Weight_Maximum, Organism, Commentary, Literature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
69000
-
-
649456
72500
calculated MW of recombinant protein expressed in Escherichia coli
210753
SplaateSubunits, Organism, Commentary, Literature
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 69278, calculated
?
-
x * 63000, SDS-PAGE, x * 65300, calculated
SplaatePosttranslational_Modification, Organism, Commentary, Literature
SplaateCommentary, Organism, Literature
SplaatepH_Stability,pH_Stability_Maximum, Organism, Commentary, Literature
SplaateTemperature_Stability,Temperature_Stability_Maximum, Organism, Commentary, Literature
SplaateGeneral_Stability, Organism, Literature
SplaateOrganic_Solvent, Organism, Commentary, Literature
SplaateOxidation_Stability,Organism,Literature
SplaateStorage_Stability, Organism, Literature
SplaateCommentary, Organism, Literature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant AcTPS2 protein is extracted and purified
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SplaateCommentary, Organism, Literature
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
mutated enzymes are generated using the QuickChange II site-directed mutagenesis kit. The PCR-based mutagenesis protocol is performed using pET200-D-TOPO harbouring the respective AcTPS2 cDNAs as template. The single-site mutant enzymes overexpressed in Escherichia coli.
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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SplaateCommentary, Organism, Literature
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression correlates well with floral volatile organic compounds emission in scented Alstroemeria genotypes
-
SplaateEngineering, Organism, Commentary, Literature
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K514A
-
AcTPS2 mutant, 90% reduction in monoterpene synthase activity compared to wild-type enzyme
K514S
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AcTPS2 mutant, presence of Ser is not able to rescue any of the activity lost after the removal of the Lys residue
SplaateCommentary, Organism, Literature
SplaateApplication,Organism,Commentary,Literature