Information on EC 4.2.3.15 - myrcene synthase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
4.2.3.15
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RECOMMENDED NAME
GeneOntology No.
myrcene synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = myrcene + diphosphate
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination, C-O bond cleavage
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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ipsdienol biosynthesis
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monoterpene biosynthesis
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Monoterpenoid biosynthesis
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oleoresin monoterpene volatiles biosynthesis
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
197462-59-2
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ORGANISM
COMMENTARY hide
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
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
(+)-limonene
show the reaction diagram
-
less than 5% of total hydrocarbon product
?
geranyl diphosphate
(-)-limonene
show the reaction diagram
-
less than 5% of total hydrocarbon product
?
geranyl diphosphate
(E)-beta-ocimene
show the reaction diagram
-
20% of total hydrocarbon product
?
geranyl diphosphate
2-carene
show the reaction diagram
-
less than 5% of total hydrocarbon product
?
geranyl diphosphate
myrcene + diphosphate
show the reaction diagram
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
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?
geranyl diphosphate
tricyclene
show the reaction diagram
-
less than 5% of total hydrocarbon product
?
linalyl diphosphate
acyclic and cyclic monoterpenes
show the reaction diagram
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-
?
neryl diphosphate
limonene
show the reaction diagram
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?
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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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
geranyl diphosphate
myrcene + diphosphate
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
required, optimum concentration of 0.5 M
Mn2+
required
additional information
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wild-type AcTPS2 is significantly more active when KCl is absent from the activity buffer
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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farnesyl diphosphate activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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farnesyl diphosphate and geranyl diphosphate activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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expression correlates well with floral volatile organic compounds emission in scented Alstroemeria genotypes
Manually annotated by BRENDA team
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young
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72500
calculated MW of recombinant protein expressed in Escherichia coli
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant AcTPS2 protein is extracted and purified
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression 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
ORGANISM
UNIPROT
LITERATURE
expression correlates well with floral volatile organic compounds emission in scented Alstroemeria genotypes
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K514A
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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