Information on EC 4.2.3.15 - myrcene synthase

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The enzyme appears in viruses and cellular organisms

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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination, C-O bond cleavage
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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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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
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
bifunctional enzyme: geranyldiphosphate synthase/myrcene synthase
SwissProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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
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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
(E)-beta-ocimene
show the reaction diagram
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20% of total hydrocarbon product
?
geranyl diphosphate
2-carene
show the reaction diagram
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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
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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
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
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