Information on EC 4.2.3.52 - (4S)-beta-phellandrene synthase (geranyl-diphosphate-cyclizing)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.3.52
-
RECOMMENDED NAME
GeneOntology No.
(4S)-beta-phellandrene synthase (geranyl-diphosphate-cyclizing)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate = (4S)-beta-phellandrene + diphosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oleoresin monoterpene volatiles biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing; (4S)-beta-phellandrene-forming]
Requires Mn2+. Mg2+ is not effective [1]. Some (-)-alpha-phellandrene is also formed [3]. The reaction involves a 1,3-hydride shift [4].
CAS REGISTRY NUMBER
COMMENTARY hide
137010-34-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
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
(4S)-beta-phellandrene + diphosphate
show the reaction diagram
neryl diphosphate
beta-phellandrene + diphosphate
show the reaction diagram
enzyme displays a clear preference for geranyl diphosphate over neryl diphosphate
in addition, enzyme produces small quantities of limonene
-
?
additional information
?
-
no substrate: farnesyl diphosphate
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cs+
-
activates
Fe2+
-
the enzyme requires either Mn2+ or Fe2+ as divalent metal ion cofactor
K+
-
activates
Mn2+
-
the enzyme requires either Mn2+ or Fe2+ as divalent metal ion cofactor, maximal activity at 1 mM MnCl2
NH4+
-
activates
Rb+
-
activates
additional information
-
no activation by Mg2+, Li+ or Na+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl dicarbonate
-
lack of substrate protection against inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00655 - 0.0078
geranyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
geranyl diphosphate
Lavandula angustifolia
E9N3U9
pH 6.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.83
geranyl diphosphate
Lavandula angustifolia
E9N3U9
pH 6.5, 30°C
175
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 8.5
-
50% of maximal activity at pH 6.6 and at pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.75
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
very poor expression
Manually annotated by BRENDA team
strong expression in young leaf
Manually annotated by BRENDA team
-
of 2-year-old Pinus contorta
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62300
x * 62300, calculated, including transit peptide, x * 62300, recombinant protein including His-Tag, SDS-PAGE
67000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 62300, calculated, including transit peptide, x * 62300, recombinant protein including His-Tag, SDS-PAGE
monomer
-
1 * 67000, SDS-PAGE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is extremely sensitive to thiol oxidation. Cyclase activity is completely lost when the partially purified xylem preparation is dialyzed against buffer (pH 7.8) devoid of thiol-protecting reagents (dithiothreitol or 2-mercaptoethanol). Other reducing agents, such as sodium ascorbate (5 mM) or sodium metabisulfite (5 mM), fail to protect the cyclases from inactivation, whereas readdition of 5 mM dithiothreitol to the dialyzed preparations restores 54% of the original activity
-
704380
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, partially purified preparation is very stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli