Information on EC 3.1.7.6 - farnesyl diphosphatase

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The enzyme appears in viruses and cellular organisms

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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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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
all-trans-farnesol biosynthesis
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juvenile hormone III biosynthesis II
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Terpenoid backbone biosynthesis
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Sesquiterpenoid and triterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphohydrolase
The enzyme is involved in the biosynthesis of acyclic sesquiterpenoids [1].
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
cv. Nakdong
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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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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-
-
-
?
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
2 mM, 2.2fold activation
Zn2+
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2 mM, 1.4fold activation
additional information
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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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-
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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
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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
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
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microsomal enzyme
6
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soluble enzyme
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
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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
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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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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x * 60000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 60000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 3.1.7.6)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)