Information on EC 4.2.3.120 - (-)-beta-pinene synthase

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The expected taxonomic range for this enzyme is: Spermatophyta

EC NUMBER
COMMENTARY hide
4.2.3.120
-
RECOMMENDED NAME
GeneOntology No.
(-)-beta-pinene synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = (-)-beta-pinene + diphosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
monoterpene biosynthesis
-
-
Monoterpenoid biosynthesis
-
-
oleoresin monoterpene volatiles biosynthesis
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-
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-beta-pinene-forming]
Cyclase II of Salvia officinalis (sage) produces about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids. The enzyme, which requires Mg2+ (preferred to Mn2+), can also use (3S)-Linalyl diphosphate (preferred to (3R)-linalyl diphosphate) [1-4]. The enzyme from Abies grandis (grand fir) produces roughly equal parts of (-)-alpha-pinene and (-)-beta-pinene [6-9]. Cyclase IV from Pinus contorta (lodgepole pine) produces 63% (-)-beta-pinene, 26% 3-carene, and traces of alpha-pinene [10]. Synthase III from Pinus taeda (loblolly pine) forms (-)-beta-pinene with traces of alpha-pinene and requires Mn2+ and K+ (Mg2+ is ineffective) [11]. A cloned enzyme from Artemisia annua (sweet wormwood) gave (-)-beta-pinene with traces of (-)-alpha-pinene [5]. The enzyme from Picea sitchensis (Sika spruce) forms 30% (-)-beta-pinene and 70% (-)-alpha-pinene [12]. See also EC 4.2.3.119, (-)-alpha-pinene synthase, EC 4.2.3.117, (-)-camphene synthase, and EC 4.2.3.107 (+)-3-carene synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
110637-20-2
for both EC 4.2.3.119 and 4.2.3.120
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
isoform synthase III
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in isoform TPS3-silenced plants, alpha-pinene, beta-pinene and beta-phellandrene contents decrease by more than 80%, whereas beta-myrcene is unchanged
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-linalyl diphosphate
(-)-beta-pinene + diphosphate
show the reaction diagram
-
-
products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
-
?
(3R)-linalyl diphosphate
myrcene + diphosphate
show the reaction diagram
-
-
-
-
?
(3S)-linalyl diphosphate
(-)-beta-pinene + diphosphate
show the reaction diagram
geranyl diphosphate
(+)-beta-pinene + diphosphate
show the reaction diagram
-
-
main product
-
?
geranyl diphosphate
(-)-beta-pinene
show the reaction diagram
-
-
products are 28% (-)-alpha-pinene, 35% (-)-beta-pinene, 24% (+)-camphene, 5% (+)-limonene, plus some terpinolene and myrcene
-
?
geranyl diphosphate
(-)-beta-pinene + diphosphate
show the reaction diagram
geranyl diphosphate
beta-pinene + diphosphate
show the reaction diagram
neryl diphosphate
(-)-beta-pinene + diphosphate
show the reaction diagram
-
-
products are (-)-alpha-pinene, (-)-beta-pinene, and (-)-camphene
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
required, Km value 7.5 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxymercuribenzoate
alpha-pinene
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-
diethyldicarbonate
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-
diphosphate
geranyl diphosphate
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substrate inhibition above 0.05 mM
N-ethylmaleimide
-
-
Phenylglyoxal
-
inactivation, coincubation with substrate and metal-ion cofactor reduces the rate of inactivation by 10-fold
phosphate
-
-
additional information
-
enzyme is inactivated by thiol-modifying agents, coincubation with substrate and metal-ion cofactor does not protect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032 - 0.0036
(3R)-linalyl diphosphate
0.001 - 0.0036
(3S)-linalyl diphosphate
0.0025 - 0.793
geranyl diphosphate
0.0023
neryl diphosphate
-
pH 7.2, 30C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019
4-hydroxymercuribenzoate
Abies grandis
-
pH 7.8, temperature not specified in the publication
0.64
diethyldicarbonate
Abies grandis
-
pH 7.8, temperature not specified in the publication
0.17
diphosphate
Abies grandis
-
pH 7.8, temperature not specified in the publication
51
phosphate
Abies grandis
-
pH 7.8, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
-
half-maximal activity
7
-
80% of maximum activity
7.9
-
half-maximal activity
8.3
-
80% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
or below, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
glants of fruit lavedo and fruit peel
Manually annotated by BRENDA team
trace expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63000
-
gel filtration
65000
-
gel fitration
95000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 62000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modeling of amino acid sequence onto the crystal structures of tobacco 5-epi-aristolochene synthase and bornyl diphosphate synthase and comparison with (-)-camphene synthase
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme, stable at 4C, in 50 mM Hepes, pH 7.8, for at least 3 weeks, at -20C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced upon wounding or methyljasmonate treatment
significant increase in transcript level in the leaders of lateral branches of weevil-attacked and mechanically wounded trees
transcript levels are transiently reduced following mechanical wounding or fungal elicitor treatment
under a photoperiod of 12 h/12 h (light/dark), the abundance of QH6 transcripts fluctuates in a diurnal pattern that ebbs around 3 h before daybreak, i.e. 9th h in the dark phase, and peaks after 9 h in light, i.e. 9th h in the light phase. The contents of (-)--pinene in juvenile leaves and in emitted volatiles also vary in a diurnal rhythm, correlating strongly with mRNA accumulation
upon methyljasmonate treatment, expression is significantly induced in medium and old leaves
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C372S
-
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C372S/C480S
-
replacement with corresponding residue of (-)-camphene synthase, 72% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W
-
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W/S485C/F597W
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replacement with corresponding residue of (-)-camphene synthase, 99% of wild-type activity. Mutant produces about 80%(-)-alpha-pinene and 10% (-)-beta-pinene
C372S/S485C
-
replacement with corresponding residue of (-)-camphene synthase, 92% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S
-
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C480S/F597W
-
replacement with corresponding residue of (-)-camphene synthase, 7% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S/S485C
-
replacement with corresponding residue of (-)-camphene synthase, 70% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
F597W
-
replacement with corresponding residue of (-)-camphene synthase, 73% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C
-
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C/F597W
-
replacement with corresponding residue of (-)-camphene synthase, 68% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
additional information
-
replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic diVerences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
renaturation after SDS-PAGE in 1% Tween 20
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