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Information on EC 3.1.7.6 - farnesyl diphosphatase
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3.1.7.6 farnesyl diphosphataseIUBMB Comments
The enzyme is involved in the biosynthesis of acyclic sesquiterpenoids .
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Word Map
- 3.1.7.6
- farnesol
- squalene
-
isopentenyl
-
geranyl
-
geranylgeranyl
-
isoprenoid
- pyrophosphate
- fdpase
-
allyl
- rice
- cholesterol
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
farnesyl diphosphatase, farnesyl pyrophosphatase, FPPase, Pho8DELTA62, pNPP/FPP phosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
farnesyl pyrophosphatase
FPPase
Pho8DELTA62
-
the purified phosphatase is a truncated Pho8 lacking 62 amino acids at the N-terminus and is designated Pho8DELTA62N
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
-
diphosphate not determined
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
-
diphosphate not determined
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
-
diphosphate not determined
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
-
diphosphate is not determined
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
-
diphosphate not determined
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
biosynthesis of acyclic sesquiterpenoids
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
diphosphate is the major product, traces of phosphate. The amount of release of diphosphate is approximately equal to the amount of release of farnesol
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
biosynthesis of acyclic sesquiterpenoids
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
the enzyme also hydrolyzes geranyl diphosphate and geranylgeranyl diphosphate to the corresponding alcohols
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
biosynthesis of acyclic sesquiterpenoids
-
-
?
(2E,6E)-farnesyl diphosphate + H2O
(2E,6E)-farnesol + diphosphate
-
biosynthesis of acyclic sesquiterpenoids
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
zaragozic acid B
-
i.e. L694,581, mixed type inhibition at 0.04 mM. No inhibition by zaragozic acid A up to 0.1 mM
geranyl diphosphate
-
16% inhibition of soluble enzyme at 0.1 mM. 26% inhibition of microsomal enzyme at 0.05 mM
geranylgeranyl diphosphate
-
0.05 mM, 16% inhibition of soluble enzyme, 38% inhibition of microsomal enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
isopentenyl diphosphate
-
20% stimulation of soluble enzyme at 0.1 mM, 20% stimulation of microsomal enzyme at 0.02 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
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
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6.8
-
pH 4.5: about 55% of maximal activity, pH 6.8: about 60% of maximal activit, soluble enzyme
5 - 6.2
-
pH 5.0: about 45% of maximal activity, pH 6.2: about 75% of maximal activity
5 - 6.8
-
pH 5.0: about 60% of maximal activity, pH 6.8: about 65% of maximal activit, microsomal enzyme
6.3 - 7
-
pH 6.3: about 80% of maximal activity, pH 7.0: about about 70% of maximal activity
7
-
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
-
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
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf
brenda
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soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf
brenda
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soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf
brenda
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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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
constitutively expressed at a high level in the soluble and the microsomal fraction
-
brenda
-
constitutively expressed at a high level in the soluble and the microsomal fraction
-
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPB_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
566
1
63004
Swiss-Prot
other Location (Reliability: 4)
A0A0C5KH39_9POAL
546
0
63085
TrEMBL
other Location (Reliability: 5)
A0A0C5KR55_9POAL
541
0
62290
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
up
-
enzyme activity increases under conditions of increased metabolic flow through the isoprenoid pathway
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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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsai, S.C.; Gaylor, J.L.
Testicular sterols. V. Preparation and partial purification of a microsomal prenol pyrophosphate pyrophophohydrolase
J. Biol. Chem.
241
4043-4050
1966
Rattus norvegicus
brenda
Ha, S.B.; Lee, D.E.; Lee, H.J.; Song, S.J.; Back, K.
Activities of soluble and microsomal farnesyl diphosphatases in Datura stramonium
Biol. Plant.
47
477-479
2003
Datura stramonium
-
brenda
Nah, J.; Song, S.J.; Back, K.
Partial characterization of farnesyl and geranylgeranyl diphosphatases induced in rice seedlings by UV-C irradiation
Plant Cell Physiol.
42
864-867
2001
Oryza sativa
brenda
Hornby, J.M.; Kebaara, B.W.; Nickerson, K.W.
Farnesol biosynthesis in Candida albicans: cellular response to sterol inhibition by zaragozic acid B
Antimicrob. Agents Chemother.
47
2366-2369
2003
Candida albicans, Candida albicans A72
brenda
Song, L.
A soluble form of phosphatase in Saccharomyces cerevisiae capable of converting farnesyl diphosphate into E,E-farnesol
Appl. Biochem. Biotechnol.
128
149-158
2006
Saccharomyces cerevisiae
brenda
Bansal, V.S.; Vaidya, S.
Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes
Arch. Biochem. Biophys.
315
393-399
1994
Rattus norvegicus
brenda
Meigs, T.E.; Simoni, R.D.
Farnesol as a regulator of HMG-CoA reductase degradation: characterization and role of farnesyl pyrophosphatase
Arch. Biochem. Biophys.
345
1-9
1997
Cricetulus griseus
brenda
Flores-Sanchez, I.J.; Ortega-Lopez, J.M.; del Carmen Montes-Horcasitas, M.; Ramos-Valdivia, A.C.
Biosynthesis of sterols and triterpenes in cell suspension cultures of Uncaria tomentosa
Plant Cell Physiol.
43
1502-1509
2002
Uncaria tomentosa
brenda
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