Welcome to LookChem.com Sign In|Join Free

CAS

  • or
Farnesyl pyrophosphate (FPP) is a 15-carbon isoprenoid that plays a crucial role in the biosynthesis of various essential compounds, such as sterols, ubiquinones, and prenylated proteins. It is synthesized from geranyl pyrophosphate (GPP) by the action of the enzyme farnesyl pyrophosphate synthase (FPPS). FPP serves as a key building block in the formation of these vital molecules, which are involved in various cellular processes and functions.

13058-04-3

Post Buying Request

13058-04-3 Suppliers

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier

13058-04-3 Usage

Uses

Used in Biomedical Research:
Farnesyl pyrophosphate is used as a prenylation agonist in human osteogenic sarcoma cells, which helps in studying the role of prenylation in collagen-based cell invasion assays. This application aids in understanding the underlying mechanisms of cancer cell invasion and metastasis.
Used in Cell Biology:
Farnesyl pyrophosphate is utilized in the prenylation of the hepatocyte growth factor (HGF) in human umbilical vein endothelial cells (HUVECs). This process is essential for the proper functioning of HGF, which is involved in various cellular processes, including cell growth, migration, and tissue repair.
Used in Enzyme Assays:
Farnesyl pyrophosphate serves as a substrate in prenyltransferases assays, which are crucial for studying the activity and function of these enzymes. These enzymes are involved in the attachment of isoprenoid groups to target proteins, a process known as prenylation, which is essential for protein function and localization.
Used in Diatom Research:
Farnesyl pyrophosphate is used in the study of diatom Haslea ostrearia, a single-celled algae that plays a significant role in aquatic ecosystems. Research on this organism can provide insights into the biochemistry and cellular processes of diatoms, which can be applied to various fields, such as biotechnology and environmental science.

Biochem/physiol Actions

Farnesyl pyrophosphate (FPP) is the precursor for the biosynthesis of cholesterol, ubiquinone and dolicol. It is part of the intracellular mevalonate pathway. FPP is essential for cell survival and is used for prenylation of several low molecular mass G proteins, including Ras. Inhibition of prenylation results in loss of oncogenic potential of Ras proteins. Inhibition of prenylation may serve as therapeutic potential for management of synaptic plasticity and Alzheimer′s disease.

Purification Methods

Purify the pyrophosphate by chromatography on Whatman No3 MM paper in a system of isopropanol-isobutanol/ammonia/water (40:20:1:30) (v/v). Store it as the Li or NH4 salt at 0o. See geranylgeranyl pyrophosphate below.

Check Digit Verification of cas no

The CAS Registry Mumber 13058-04-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,3,0,5 and 8 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 13058-04:
(7*1)+(6*3)+(5*0)+(4*5)+(3*8)+(2*0)+(1*4)=73
73 % 10 = 3
So 13058-04-3 is a valid CAS Registry Number.
InChI:InChI=1/C15H28O7P2/c1-13(2)7-5-8-14(3)9-6-10-15(4)11-12-21-24(19,20)22-23(16,17)18/h7,9,11H,5-6,8,10,12H2,1-4H3,(H,19,20)(H2,16,17,18)/b14-9+,15-11+

13058-04-3SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name farnesyl diphosphate

1.2 Other means of identification

Product number -
Other names FARNESYLPYROPHOSPHATE

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:13058-04-3 SDS

13058-04-3Synthetic route

(2E,6E)-1-Bromo-3,7,11-trimethyl-dodeca-2,6,10-triene
6874-67-5

(2E,6E)-1-Bromo-3,7,11-trimethyl-dodeca-2,6,10-triene

Farnesyl Pyrophosphate
13058-04-3

Farnesyl Pyrophosphate

Conditions
ConditionsYield
With tris(tetra-n-butylammonium) hydrogen pyrophosphate In acetonitrile for 24h; Ambient temperature; Yield given;
farnesyl alcohol
82010-11-5

farnesyl alcohol

Farnesyl Pyrophosphate
13058-04-3

Farnesyl Pyrophosphate

Conditions
ConditionsYield
Multi-step reaction with 2 steps
1: PBr3 / pentane / 0.17 h / 0 °C
2: Tris(tetra-n-butylammonium) Hydrogen Pyrophosphate / acetonitrile / 24 h / Ambient temperature
View Scheme

13058-04-3Related news

[20] Purification of FARNESYLPYROPHOSPHATE (cas 13058-04-3) synthetase by affinity chromatography09/24/2019

Publisher SummaryThis chapter describes the synthesis of an affinity column for farnesylpyrophosphate synthetase based on the geranyl moiety and a rapid purification of the enzyme from avian liver and yeast. Farnesylpyrophosphate synthetase is a 1'-4 prenyltransferase that produces a key in...detailed

Inhibition of FARNESYLPYROPHOSPHATE (cas 13058-04-3) synthase prevents angiotensin II-induced hypertrophic responses in rat neonatal cardiomyocytes: Involvement of the RhoA/Rho kinase pathway09/09/2019

The RhoA/Rho-kinase (ROCK) pathway is involved in angiotensin (Ang) II-induced cardiac hypertrophy. However, it is still unclear whether inhibition of farnesylpyrophosphate (FPP) synthase can attenuate Ang II-induced hypertrophic responses, and whether it involves the RhoA/ROCK pathway. The anti...detailed

Knockdown of FARNESYLPYROPHOSPHATE (cas 13058-04-3) synthase prevents angiotensin II-mediated cardiac hypertrophy09/08/2019

The Rho guanosine triphosphatases (Rho GTPases) family, including RhoA, plays an important role in angiotensin II (Ang II)-mediated cardiac hypertrophy. Farnesylpyrophosphate synthase (FPPS)-catalyzed isoprenoid intermediates are vital for activation of RhoA. The present study was designed to in...detailed

13058-04-3Relevant articles and documents

THE ABSOLUTE STEREOCHEMISTRY OF THE ENZYMIC CYCLISATION TO FORM THE STERPURENE SESQUITERPENES

Abell, Chris,Leech, Andrew P.

, p. 4337 - 4340 (1988)

Incorporation studies using acetate into a novel sterpurene sesquiterpene, 9,12-dihydroxysterpurene (1), have allowed the absolute stereochemistry of the enzymic cyclisation of farnesyl pyrophosphate to sterpurene to be elucidated.Observation of two-bond 13C-13C coupling across the cyclobutane ring confirms the derivation of these two carbon atoms from the same acetate unit.

Biosynthesis of isoprenoids in Escherichia coli: stereochemistry of the reaction catalyzed by farnesyl diphosphate synthase.

Leyes,Baker,Poulter

, p. 1071 - 1073 (1999)

[formula: see text] Farnesyl diphosphate (FPP) synthase from Escherichia coli catalyzes the condensation of isopentenyl diphosphate (IPP) and geranyl diphosphate (GPP) with selective removal of the pro-R hydrogen at C2 of IPP, the same stereochemistry observed for the pig liver, yeast, and avian enzymes.

Mycobacterium tuberculosis H37Rv3377c encodes the diterpene cyclase for producing the halimane skeleton

Nakano, Chiaki,Okamura, Tomoo,Sato, Tsutomu,Dairi, Tohru,Hoshino, Tsutomu

, p. 1016 - 1018 (2005)

The cloning and functional expression of Mycobacterium tuberculosis Rv3377c in Escherichia coli revealed that this gene encodes the diterpene cyclase for producing (+)-5(6),13-halimadiene-15-ol, which accepts geranylgeranyldiphosphate as the intrinsic substrate. The Royal Society of Chemistry 2005.

Incorporation of farnesyl pyrophosphate derivertives into abscisic acid and its biosynthetic intermediates in Cercospora cruenta

Yamamoto, Hirotaka,Oritani, Takayuki

, p. 821 - 824 (1997)

To investigate the transformation from (2E,6E)-farnesyl pyrophosphate to (2Z,4E)-γ-ionylideneethanol in the abscisic acid-producing fungi, Cercospora cruenta, plausible [2-14C]-C15 intermediates were prepared and fed. Substrates such as (2E,6E)-farnesyl pyrophosphate, (2Z,4E)-γ-ionylideneethanol and its pyrophosphate were incorporated into ABA and its known biosynthetic precursors. It is suggested that (2E,6E)-farnesyl pyrophosphate is converted to (2Z,4E)-γ-ionylideneethanol in four consecutive steps: dehydrogenation, isomerization, cyclization and hydrolysis.

Cloning and characterization of isoprenyl diphosphate synthases with farnesyl diphosphate and geranylgeranyl diphosphate synthase activity from Norway spruce (Picea abies) and their relation to induced oleoresin formation

Schmidt, Axel,Gershenzon, Jonathan

, p. 2649 - 2659 (2007)

The conifer Picea abies (Norway spruce) employs terpenoid-based oleoresins as part of its constitutive and induced defense responses to herbivores and pathogens. The isoprenyl diphosphate synthases are branch-point enzymes of terpenoid biosynthesis leading to the various terpene classes. We isolated three genes encoding isoprenyl diphosphate synthases from P. abies cDNA libraries prepared from the bark and wood of methyl jasmonate-treated saplings and screened via a homology-based PCR approach using degenerate primers. Enzyme assays of the purified recombinant proteins expressed in Escherichia coli demonstrated that one gene (PaIDS 4) encodes a farnesyl diphosphate synthase and the other two (PaIDS 5 and PaIDS 6) encode geranylgeranyl diphosphate synthases. The sequences have moderate similarity to those of farnesyl diphosphate and geranylgeranyl diphosphate synthases already known from plants, and the kinetic properties of the enzymes are not unlike those of other isoprenyl diphosphate synthases. Of the three genes, only PaIDS 5 displayed a significant increase in transcript level in response to methyl jasmonate spraying, suggesting its involvement in induced oleoresin biosynthesis.

Synthesis of geranyl S-thiolodiphosphate. A new alternative substrate/inhibitor for prenyltransferases.

Phan,Poulter

, p. 2287 - 2289 (2000)

The tris(tetra-n-butylammonium) salt of thiopyrophosphate 5 was prepared from trimethyl phosphate in four steps. Treatment of geranyl bromide with 5 gave an 80% yield of geranyl S-thiolodiphosphate (6). Thiolodiphosphate 6 is substantially less reactive than geranyl diphosphate (7) in the prenyl transfer reaction catalyzed by farnesyl diphosphate synthase and is a good inhibitor of the enzyme.

Tris(tetra-n-butylammonium) hydrogen pyrophosphate. A new reagent for the preparation of allylic pyrophosphate esters [3]

Dixit, Vyas M.,Laskovics, F. Mark,Noall, Wendy I.,Poulter, C. Dale

, p. 1967 - 1969 (1981)

Tris(tetra-n-butylammonium) hydrogen pyrophosphate was used to prepare dimethylallyl pyrophosphate (1-OPP), 7-methylocta-2,6-dien-1-yl pyrophosphate (2-OPP), geranyl pyrophosphate (3-OPP), 2-flourogeranyl pyrophosphate (4-OPP), and farnesyl pyrophosphate (5-OPP) from the corresponding alcohols in moderate yields by a two-step sequence via the corresponding primary, allylic bromides.

Mutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates

Dellas, Nikki,Noel, Joseph P.

, p. 589 - 601 (2010)

The biosynthesis of isopentenyl diphosphate (IPP) from either the mevalonate (MVA) or the 1-deoxy-d-xylulose 5-phosphate (DXP) pathway provides the key metabolite for primary and secondary isoprenoid biosynthesis. Isoprenoid metabolism plays crucial roles in membrane stability, steroid biosynthesis, vitamin production, protein localization, defense and communication, photoprotection, sugar transport, and glycoprotein biosynthesis. Recently, an alternative branch of the MVA pathway was discovered in the archaeon Methanocaldococcus jannaschii involving a small molecule kinase, isopentenyl phosphate kinase (IPK). IPK belongs to the amino acid kinase (AAK) superfamily. In vitro, IPK phosphorylates isopentenyl monophosphate (IP) in an ATP and Mg2+-dependent reaction producing IPP. Here, we describe crystal structures of IPK from M. jannaschii refined to nominal resolutions of 2.0-2.8 A. Notably, an active site histidine residue (His60) forms a hydrogen bond with the terminal phosphate of both substrate and product. This His residue serves as a marker for a subset of the AAK family that catalyzes phosphorylation of phosphate or phosphonate functional groups; the larger family includes carboxyl-directed kinases, which lack this active site residue. Using steady-state kinetic analysis of H60A, H60N, and H60Q mutants, the protonated form of the Nε2 nitrogen of His60 was shown to be essential for catalysis, most likely through hydrogen bond stabilization of the transition state accompanying transphosphorylation. Moreover, the structures served as the starting point for the engineering of IPK mutants capable of the chemoenzymatic synthesis of longer chain isoprenoid diphosphates from monophosphate precursors.

Structure-based protein engineering enables prenyl donor switching of a fungal aromatic prenyltransferase

Mai, Peter,Zocher, Georg,Stehle, Thilo,Li, Shu-Ming

, p. 7461 - 7469 (2018)

Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few such enzymes can use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) as donors. This catalytic gap prohibits the wide application of PTs for structural diversification. Structure-guided molecular modelling and site-directed mutagenesis of FgaPT2 from Aspergillus fumigatus led to the identification of the gatekeeping residue Met328 responsible for the prenyl selectivity and sets the basis for creation of GPP- and FPP-accepting enzymes. Site-saturation mutagenesis of the gatekeeping residue at position 328 in FgaPT2 revealed that the size of this side chain is the determining factor for prenyl selectivity, while its hydrophobicity is crucial for allowing DMAPP and GPP to bind.

Farnesyl Diphosphate Synthase Reactions of Geranyl Diphosphate Analogues Having Oxygen Atoms in Their Alkyl Chains

Maki, Yuji,Satoh, Hikaru,Kurihara, Masayo,Endo, Takae,Watanabe, Gotaro,Ogura, Kyozo

, p. 1841 - 1844 (1994)

Seven geranyl diphosphate analogues having oxygen atoms in their alkyl chains were synthesized and examined for their reactivities as substrates in the reaction catalyzed by pig liver farnesyl diphosphate synthase.All of these compounds acted as substrates to give farnesyl diphosphate analogues.It was suggested that the enzyme cavity for the geranyl moiety is tolerant enough to accommodate alkyl moietes containing oxygen atoms.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1

What can I do for you?
Get Best Price

Get Best Price for 13058-04-3