Information on EC 3.1.7.6 - farnesyl diphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.7.6
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RECOMMENDED NAME
GeneOntology No.
farnesyl diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
all-trans-farnesol biosynthesis
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Biosynthesis of secondary metabolites
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juvenile hormone III biosynthesis II
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Sesquiterpenoid and triterpenoid biosynthesis
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Terpenoid backbone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphohydrolase
The enzyme is involved in the biosynthesis of acyclic sesquiterpenoids [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain A72
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Manually annotated by BRENDA team
strain A72
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cv. Nakdong
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Manually annotated by BRENDA team
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-
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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
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
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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
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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2 mM, 2.2fold activation
Zn2+
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2 mM, 1.4fold activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienoic acid
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(2E,6E)-farnesyl diphosphate
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competitive
3',5'-cAMP
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arsenite
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1 mM
farnesyl diphosphate
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0.25 mM, 80% inhibition
farnesyl monophosphate
geranyl diphosphate
geranylgeranyl diphosphate
isopentenyl diphosphate
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competitive
Mg2+
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2 mM, 92% inhibition. 0.06 mM, no inhibition
Mn2+
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2 mM, 93% inhibition
NaF
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100 mM, about 70% inhibition
phosphate
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2 mM, 85% inhibition
Plasma albumin
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zaragozic acid B
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i.e. L694,581, mixed type inhibition at 0.04 mM. No inhibition by zaragozic acid A up to 0.1 mM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
isopentenyl diphosphate
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20% stimulation of soluble enzyme at 0.1 mM, 20% stimulation of microsomal enzyme at 0.02 mM
p-nitrophenyl phosphate
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0.05, 10% stimulation
Triton X-100
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0.05 g/l, stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 1.2
(2E,6E)-farnesyl diphosphate
additional information
additional information
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the KM-value for (2E,6E)-farnesyl diphosphate increases with an increase in pH
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37
(2E,6E)-farnesyl diphosphate
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pH 5.5, 37°C
0.1
geranyl diphosphate
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0.005
geranylgeranyl diphosphate
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5.2
isopentenyl diphosphate
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pH 8.8, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
farnesyl monophosphate
Rattus norvegicus
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pH 5.5, 37°C
0.005
geranylgeranyl diphosphate
Rattus norvegicus
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pH 5.5, 37°C
0.02
zaragozic acid B
Rattus norvegicus
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
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microsomal enzyme
6
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soluble enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6.8
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pH 4.5: about 55% of maximal activity, pH 6.8: about 60% of maximal activit, soluble enzyme
5 - 6.8
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pH 5.0: about 60% of maximal activity, pH 6.8: about 65% of maximal activit, microsomal enzyme
5 - 6.2
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pH 5.0: about 45% of maximal activity, pH 6.2: about 75% of maximal activity
6.3 - 7
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pH 6.3: about 80% of maximal activity, pH 7.0: about about 70% of maximal activity
7
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maximal activity at pH 7.0, less than 1% of maximal activity at pH 6.0, less than 10% of maximal activity at pH 8.5
8.5 - 9.1
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pH 8.5: about 40% of maximal activity, pH 9.1: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf
Manually annotated by BRENDA team
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soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf
Manually annotated by BRENDA team
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soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf
Manually annotated by BRENDA team
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soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf. Root has the highest level of microsomal enzyme
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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constitutively expressed at a high level in the soluble and the microsomal fraction
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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x * 60000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 60000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
constitutively expressed at a high level in the soluble and the microsomal fraction
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maximally induced 36 h after UV-C irradiation and decreased until 60 h
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the flux of farnesyl diphosphate to farnesol is two times lower in cells elicited with pectin treatment than in control cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
up
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enzyme activity increases under conditions of increased metabolic flow through the isoprenoid pathway