Information on EC 4.2.3.10 - (-)-endo-fenchol synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.3.10
-
RECOMMENDED NAME
GeneOntology No.
(-)-endo-fenchol synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranyl diphosphate + H2O = (-)-endo-fenchol + diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P-O bond cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
fenchol biosynthesis I
-
-
fenchol biosynthesis II
-
-
fenchone biosynthesis
-
-
Monoterpenoid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-endo-fenchol-forming]
(3R)-Linalyl diphosphate is an intermediate in the reaction
CAS REGISTRY NUMBER
COMMENTARY hide
117758-41-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
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
2,3-cyclopropylgeranyl diphosphate
?
show the reaction diagram
-
at 53% of the rate of conversion of geranyl diphosphate, formation of ether-soluble products
-
-
?
6,7-dihydrogeranyl diphosphate
?
show the reaction diagram
-
at 35% of the rate of conversion of geranyl diphosphate, formation of ether-soluble products
-
-
?
dimethylallyl diphosphate
dimethylallyl alcohol + diphosphate
show the reaction diagram
-
at the same rate as the cyclization of geranyl diphosphate
-
?
farnesyl diphosphate
?
show the reaction diagram
-
at 25% of the rate of conversion of geranyl diphosphate, formation of ether-soluble products
-
-
?
geranyl diphosphate
(-)-endo-fenchol + diphosphate
show the reaction diagram
geranyl diphosphate + H2O
alpha-fenchol + diphosphate
show the reaction diagram
additional information
?
-
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
(-)-endo-fenchol + diphosphate
show the reaction diagram
additional information
?
-
-
monoterpene biosynthesis
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
metal ion-dependent
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-cyclopropylgeranyl diphosphate
-
competitive inhibitor
2-Fluorogeranyl diphosphate
-
effective competitive inhibitor
2-Fluorolinalyl diphosphate
-
effective competitive inhibitor
6,7-dihydrogeranyl diphosphate
-
competitive inhibitor
diethyl dicarbonate
-
inhibition is reversed by hydroxylamine
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
2,3-cyclopropylgeranyl diphosphate
-
pH 6.5, 30°C
0.025
6,7-dihydrogeranyl diphosphate
-
pH 6.5, 30°C
0.006
geranyl diphosphate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
2,3-cyclopropylgeranyl diphosphate
-
pH 6.5, 30°C
0.01
2-Fluorogeranyl diphosphate
-
pH 6.5, 30°C
0.013
2-Fluorolinalyl diphosphate
-
pH 6.5, 30°C
0.04
6,7-dihydrogeranyl diphosphate
-
pH 6.5, 30°C
additional information
additional information
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
schizocarps
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no significant difference in the kinetics of inactivation up to 50°C of free and immobilized enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme form is markedly more stable than the free form
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, immobilized enzyme on CH-activated Sepharose, 1 month, retains over 30% of the original activity, the activity of the free enzyme is negligible
-
4°C, immobilized enzyme on CH-activated Sepharose, in presence of 1 mM sodium diphosphate as substrate analog, 1 month, retains over 60% of the original activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichi coli