Information on EC 3.1.7.6 - farnesyl diphosphatase

Substrates: biosynthesis of acyclic sesquiterpenoids
Products: -

(2E,6E)-farnesyl diphosphate + H2O

(2E,6E)-farnesol + diphosphate

Substrates: the enzyme also hydrolyzes geranyl diphosphate and geranylgeranyl diphosphate to the corresponding alcohols
Products: -

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

(2E,6E)-farnesyl diphosphate + H2O

(2E,6E)-farnesol + diphosphate

3 entries

(2E,6E)-farnesyl diphosphate + H2O

(2E,6E)-farnesol + diphosphate

Substrates: -
Products: -

(2E,6E)-farnesyl diphosphate + H2O

(2E,6E)-farnesol + diphosphate

Substrates: biosynthesis of acyclic sesquiterpenoids
Products: -

(2E,6E)-farnesyl diphosphate + H2O

(2E,6E)-farnesol + diphosphate

Substrates: biosynthesis of acyclic sesquiterpenoids
Products: -

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ca2+

2 mM, 2.2fold activation

Mg2+

Zn2+

2 mM, 1.4fold activation

additional information

Mg2+

slight stimulation

Mg2+

activity is dependent on

706169

additional information

Mg2+-independent enzyme

additional information

Mg2+-independent enzyme

additional information

the activity is metal ion independent

additional information

2 mM CuSO4 shows no effect

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienoic acid

(2E,6E)-farnesyl diphosphate

competitive

3',5'-cAMP

arsenite

1 mM

farnesyl diphosphate

0.25 mM, 80% inhibition

farnesyl monophosphate

geranyl diphosphate

geranylgeranyl diphosphate

4 entries

isopentenyl diphosphate

competitive

Mg2+

2 mM, 92% inhibition. 0.06 mM, no inhibition

Mn2+

2 mM, 93% inhibition

NaF

100 mM, about 70% inhibition

phosphate

2 mM, 85% inhibition

Plasma albumin

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

additional information

farnesyl monophosphate

0.07 mM, 35% inhibition

farnesyl monophosphate

geranyl diphosphate

16% inhibition of soluble enzyme at 0.1 mM. 26% inhibition of microsomal enzyme at 0.05 mM

geranyl diphosphate

geranylgeranyl diphosphate

0.05 mM, 60% inhibition

geranylgeranyl diphosphate

0.05 mM, 16% inhibition of soluble enzyme, 38% inhibition of microsomal enzyme

geranylgeranyl diphosphate

geranylgeranyl diphosphate

potent noncompetitive inhibitor

additional information

no inhibition by 1 mM p-mercuribenzoate

additional information

2 mM CuSO4 shows no effect

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

ATP

isopentenyl diphosphate

20% stimulation of soluble enzyme at 0.1 mM, 20% stimulation of microsomal enzyme at 0.02 mM

p-nitrophenyl phosphate

0.05, 10% stimulation

Triton X-100

show all columns Go to KM Value Search

0.05 g/l, stimulates

ATP

0.05, 8% stimulation

ATP

0.93 mM, stimulates

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.007 - 1.2

(2E,6E)-farnesyl diphosphate

3 entries

additional information

the KM-value for (2E,6E)-farnesyl diphosphate increases with an increase in pH

0.007

(2E,6E)-farnesyl diphosphate

pH 5.5, 37°C

0.015

(2E,6E)-farnesyl diphosphate

pH 5.5, 37°C

0.7 - 1.2

(2E,6E)-farnesyl diphosphate

pH 8.8, 37°C

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.37

(2E,6E)-farnesyl diphosphate

pH 5.5, 37°C

0.1

geranyl diphosphate

0.005

geranylgeranyl diphosphate

5.2

isopentenyl diphosphate

pH 8.8, 37°C

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.07

farnesyl monophosphate

Rattus norvegicus

pH 5.5, 37°C

0.005

geranylgeranyl diphosphate

Rattus norvegicus

pH 5.5, 37°C

0.02

zaragozic acid B

Rattus norvegicus

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.0068

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.2

microsomal enzyme

5.5

soluble enzyme

6.8

show all columns Go to pH Range Search

8.8

5.5

assay at

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

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

show all columns Go to Organism Search

assay at

assay at

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

brenda

brenda

brenda

cv. Nakdong

brenda

brenda

show all columns Go to Source Tissue Search

brenda

brenda

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

cell suspension culture

brenda

soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf

brenda

fruit

soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf

brenda

leaf

show all columns Go to Localization Search

soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf

brenda

brenda

soluble farnesyl diphosphatase is highest in fruit and flower followed by root and leaf. Root has the highest level of microsomal enzyme

brenda

brenda

brenda

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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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

microsome

constitutively expressed at a high level in the soluble and the microsomal fraction

brenda

brenda

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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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).

Q84ZW8 pBLAST

ACSS_MAIZE

Zea mays

590

67328

Swiss-Prot

Chloroplast (Reliability: 5)

P11491 pBLAST

PPB_YEAST

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

566

63004

Swiss-Prot

other Location (Reliability: 4)

O06728 pBLAST

YISP_BACSU

Bacillus subtilis (strain 168)

267

30621

Swiss-Prot

A0A0H4P3T2 pBLAST

A0A0H4P3T2_9BACI

Bacillus smithii

526

58160

TrEMBL

A0A0C5KH39 pBLAST

A0A0C5KH39_PHYED

Phyllostachys edulis

546

63085

TrEMBL

other Location (Reliability: 5)

A0A0C5KR55 pBLAST

A0A0C5KR55_PHYED

Phyllostachys edulis

541

62290

TrEMBL

other Location (Reliability: 3)

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

60000

x * 60000, SDS-PAGE

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

x * 60000, SDS-PAGE

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

enzyme activity increases under conditions of increased metabolic flow through the isoprenoid pathway

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

partial

Go to Expression Search

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

constitutively expressed at a high level in the soluble and the microsomal fraction

maximally induced 36 h after UV-C irradiation and decreased until 60 h

top print hide References Search

the flux of farnesyl diphosphate to farnesol is two times lower in cells elicited with pectin treatment than in control cells

Uncaria tomentosa

706169

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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

4288361

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.

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.

864-867

2001

Oryza sativa

11522913

brenda

701723

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.

2366-2369

2003

Candida albicans, Candida albicans A72

12821501

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

16484724

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

7986083

brenda