Farnesyl diphosphate

Farnesyl diphosphate is a lipid of Prenol Lipids (PR) class. Farnesyl diphosphate is associated with abnormalities such as Dental caries and Hyperostosis, Diffuse Idiopathic Skeletal. The involved functions are known as Regulation, Process, Signal, Anabolism and inhibitors. Farnesyl diphosphate often locates in peroxisome, Cytoplasmic matrix, Plasma membrane, soluble and Mitochondria. The associated genes with Farnesyl diphosphate are HSD3B1 gene, ABRA gene, MATN1 gene, SEPSECS gene and MBD2 gene. The related lipids are Sterols, 22-hydroxycholesterol, dehydrosqualene, SK&F 104976 and 25-hydroxycholesterol.

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Introduction

To understand associated biological information of Farnesyl diphosphate, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Farnesyl diphosphate?

Farnesyl diphosphate is suspected in and other diseases in descending order of the highest number of associated sentences.

Related references are mostly published in these journals:

Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Farnesyl diphosphate

MeSH term MeSH ID Detail
Adenocarcinoma D000230 166 associated lipids
Colonic Neoplasms D003110 161 associated lipids
Osteosarcoma D012516 50 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Hypercholesterolemia D006937 91 associated lipids
Liver Neoplasms, Experimental D008114 46 associated lipids
Endometriosis D004715 29 associated lipids
Leukemia, Myeloid D007951 52 associated lipids
Leukemia-Lymphoma, Adult T-Cell D015459 25 associated lipids
Protozoan Infections D011528 6 associated lipids
Total 10

PubChem Associated disorders and diseases

What pathways are associated with Farnesyl diphosphate

Lipid pathways are not clear in current pathway databases. We organized associated pathways with Farnesyl diphosphate through full-text articles, including metabolic pathways or pathways of biological mechanisms.

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PubChem Biomolecular Interactions and Pathways

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What cellular locations are associated with Farnesyl diphosphate?

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What functions are associated with Farnesyl diphosphate?


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What lipids are associated with Farnesyl diphosphate?

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What genes are associated with Farnesyl diphosphate?

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Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with Farnesyl diphosphate?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Farnesyl diphosphate

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Authors Title Published Journal PubMed Link
Hua L and Matsuda SP The molecular cloning of 8-epicedrol synthase from Artemisia annua. 1999 Arch. Biochem. Biophys. pmid:10486139
Mercke P et al. Cloning, expression, and characterization of epi-cedrol synthase, a sesquiterpene cyclase from Artemisia annua L. 1999 Arch. Biochem. Biophys. pmid:10486140
Bansal VS and Vaidya S Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes. 1994 Arch. Biochem. Biophys. pmid:7986083
Thompson JF et al. Truncation of human squalene synthase yields active, crystallizable protein. 1998 Arch. Biochem. Biophys. pmid:9473303
Chang YJ et al. Amorpha-4,11-diene synthase of Artemisia annua: cDNA isolation and bacterial expression of a terpene synthase involved in artemisinin biosynthesis. 2000 Arch. Biochem. Biophys. pmid:11185551
Picaud S et al. Amorpha-4,11-diene synthase: mechanism and stereochemistry of the enzymatic cyclization of farnesyl diphosphate. 2006 Arch. Biochem. Biophys. pmid:16143293
Mercke P et al. Molecular cloning, expression, and characterization of amorpha-4,11-diene synthase, a key enzyme of artemisinin biosynthesis in Artemisia annua L. 2000 Arch. Biochem. Biophys. pmid:11032404
Schulte AE et al. Purification and characterization of mevalonate kinase from suspension-cultured cells of Catharanthus roseus (L.) G. Don. 2000 Arch. Biochem. Biophys. pmid:10860546
Croteau R et al. Biosynthesis of the sesquiterpene patchoulol from farnesyl pyrophosphate in leaf extracts of Pogostemon cablin (patchouli): mechanistic considerations. 1987 Arch. Biochem. Biophys. pmid:3038029
Dehal SS and Croteau R Partial purification and characterization of two sesquiterpene cyclases from sage (Salvia officinalis) which catalyze the respective conversion of farnesyl pyrophosphate to humulene and caryophyllene. 1988 Arch. Biochem. Biophys. pmid:3355155
Cane DE and Pargellis C Partial purification and characterization of pentalenene synthase. 1987 Arch. Biochem. Biophys. pmid:3579312
Hohn TM and Plattner RD Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti. 1989 Arch. Biochem. Biophys. pmid:2544140
Okada S et al. Characterization of botryococcene synthase enzyme activity, a squalene synthase-like activity from the green microalga Botryococcus braunii, Race B. 2004 Arch. Biochem. Biophys. pmid:14725863
Chen XY et al. Cloning, expression, and characterization of (+)-delta-cadinene synthase: a catalyst for cotton phytoalexin biosynthesis. 1995 Arch. Biochem. Biophys. pmid:8554317
Cane DE et al. Overproduction of soluble trichodiene synthase from Fusarium sporotrichioides in Escherichia coli. 1993 Arch. Biochem. Biophys. pmid:8424673
Croteau R and Gundy A Cyclization of farnesyl pyrophosphate to the sesquiterpene olefins humulene and caryophyllene by an enzyme system from sage (Salvia officinalis). 1984 Arch. Biochem. Biophys. pmid:6486812
Little DB and Croteau RB Alteration of product formation by directed mutagenesis and truncation of the multiple-product sesquiterpene synthases delta-selinene synthase and gamma-humulene synthase. 2002 Arch. Biochem. Biophys. pmid:12051690
Schmidt CO et al. Isolation, characterization, and mechanistic studies of (-)-alpha-gurjunene synthase from Solidago canadensis. 1999 Arch. Biochem. Biophys. pmid:10190971
Sánchez De Cos Escuín J [New therapeutic targets and strategies in lung cancer]. 2002 Arch. Bronconeumol. pmid:12199921
Zhang YL and Li ZX Functional analysis and molecular docking identify two active short-chain prenyltransferases in the green peach aphid, Myzus persicae. 2012 Arch. Insect Biochem. Physiol. pmid:22696503
Vincent L et al. Cerivastatin, an inhibitor of 3-hydroxy-3-methylglutaryl coenzyme a reductase, inhibits endothelial cell proliferation induced by angiogenic factors in vitro and angiogenesis in in vivo models. 2002 Arterioscler. Thromb. Vasc. Biol. pmid:11950701
Bourcier T and Libby P HMG CoA reductase inhibitors reduce plasminogen activator inhibitor-1 expression by human vascular smooth muscle and endothelial cells. 2000 Arterioscler. Thromb. Vasc. Biol. pmid:10669656
Deakin S et al. Simvastatin modulates expression of the PON1 gene and increases serum paraoxonase: a role for sterol regulatory element-binding protein-2. 2003 Arterioscler. Thromb. Vasc. Biol. pmid:14500290
Blanco-Colio LM et al. 3-Hydroxy-3-methyl-glutaryl coenzyme A reductase inhibitors, atorvastatin and simvastatin, induce apoptosis of vascular smooth muscle cells by downregulation of Bcl-2 expression and Rho A prenylation. 2002 Atherosclerosis pmid:11882313
Kaneta S et al. All hydrophobic HMG-CoA reductase inhibitors induce apoptotic death in rat pulmonary vein endothelial cells. 2003 Atherosclerosis pmid:14612203
Dull BJ et al. The modulating effect of an inhibitor of cholesterolgenesis present in bovine milk upon the synthesis of cholesterol, dolichol and ubiquinone. 1983 Atherosclerosis pmid:6661267
Fukuyama R et al. Statins inhibit osteoblast migration by inhibiting Rac-Akt signaling. 2004 Biochem. Biophys. Res. Commun. pmid:14975748
Solomon CS and Goalstone ML Dominant negative farnesyltransferase alpha-subunit inhibits insulin mitogenic effects. 2001 Biochem. Biophys. Res. Commun. pmid:11444820
Okamoto T et al. Incadronate disodium inhibits advanced glycation end products-induced angiogenesis in vitro. 2002 Biochem. Biophys. Res. Commun. pmid:12237136
ANDERSON DG et al. The conversion of farnesyl pyrophosphate to squalene by soluble extracts of microsomes. 1960 Biochem. Biophys. Res. Commun. pmid:13683185
Wiemer AJ et al. Digeranyl bisphosphonate inhibits geranylgeranyl pyrophosphate synthase. 2007 Biochem. Biophys. Res. Commun. pmid:17208200
Wada H et al. Statins activate GATA-6 and induce differentiated vascular smooth muscle cells. 2008 Biochem. Biophys. Res. Commun. pmid:18671946
Westfall D et al. Metabolism of farnesol: phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions. 1997 Biochem. Biophys. Res. Commun. pmid:9015362
Runquist M et al. Biosynthesis of trans,trans,trans-geranylgeranyl diphosphate by the cytosolic fraction from rat tissues. 1992 Biochem. Biophys. Res. Commun. pmid:1632765
Mbaya B et al. Isoprenoid metabolism in Plasmodium falciparum during the intraerythrocytic phase of malaria. 1990 Biochem. Biophys. Res. Commun. pmid:2268347
Yoshida I et al. Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26. 1989 Biochem. Biophys. Res. Commun. pmid:2541701
Lu YP et al. Mechanism of cis-prenyltransferase reaction probed by substrate analogues. 2010 Biochem. Biophys. Res. Commun. pmid:20828539
Das NP and Allen CM Inhibition of farnesyl transferases from malignant and non-malignant cultured human lymphocytes by prenyl substrate analogues. 1991 Biochem. Biophys. Res. Commun. pmid:1755854
Lu YP et al. Different reaction mechanisms for cis- and trans-prenyltransferases. 2009 Biochem. Biophys. Res. Commun. pmid:19103164
Tatsuno I et al. Geranylgeranylpyrophosphate, a metabolite of mevalonate, regulates the cell cycle progression and DNA synthesis in human lymphocytes. 1997 Biochem. Biophys. Res. Commun. pmid:9425279
M'Baya B and Karst F In vitro assay of squalene epoxidase of Saccharomyces cerevisiae. 1987 Biochem. Biophys. Res. Commun. pmid:3307781
Cao L et al. An insect farnesyl phosphatase homologous to the N-terminal domain of soluble epoxide hydrolase. 2009 Biochem. Biophys. Res. Commun. pmid:19168029
Sagami H et al. Novel isoprenoid modified proteins in Halobacteria. 1994 Biochem. Biophys. Res. Commun. pmid:8093082
Ishii K et al. Decaprenyl pyrophosphate synthetase from mitochondria of pig liver. 1983 Biochem. Biophys. Res. Commun. pmid:6651825
Lee SK et al. Stabilization and translocation of p53 to mitochondria is linked to Bax translocation to mitochondria in simvastatin-induced apoptosis. 2010 Biochem. Biophys. Res. Commun. pmid:20043868
Edelstein RL and Distefano MD Photoaffinity labeling of yeast farnesyl protein transferase and enzymatic synthesis of a Ras protein incorporating a photoactive isoprenoid. 1997 Biochem. Biophys. Res. Commun. pmid:9199201
Keller RK and Fliesler SJ Mechanism of aminobisphosphonate action: characterization of alendronate inhibition of the isoprenoid pathway. 1999 Biochem. Biophys. Res. Commun. pmid:10600541
Danesi R et al. Specific labeling of isoprenylated proteins: application to study inhibitors of the post-translational farnesylation and geranylgeranylation. 1995 Biochem. Biophys. Res. Commun. pmid:7826382
Chen AP et al. Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase. 2005 Biochem. J. pmid:15447632
Goto T et al. Farnesyl pyrophosphate regulates adipocyte functions as an endogenous PPARγ agonist. 2011 Biochem. J. pmid:21605082
Brown AJ Isoprenoid is a perfect fit for fat factor. 2011 Biochem. J. pmid:21793802
Cohen LH et al. Inhibition of human smooth muscle cell proliferation in culture by farnesyl pyrophosphate analogues, inhibitors of in vitro protein: farnesyl transferase. 1999 Biochem. Pharmacol. pmid:9933024
Sillero MA et al. Synthesis of ATP derivatives of compounds of the mevalonate pathway (isopentenyl di- and triphosphate; geranyl di- and triphosphate, farnesyl di- and triphosphate, and dimethylallyl diphosphate) catalyzed by T4 RNA ligase, T4 DNA ligase and other ligases Potential relationship with the effect of bisphosphonates on osteoclasts. 2009 Biochem. Pharmacol. pmid:19414000
Cohen LH et al. Different analogues of farnesyl pyrophosphate inhibit squalene synthase and protein:farnesyltransferase to different extents. 1995 Biochem. Pharmacol. pmid:7702642
Hartmann MA et al. Metabolism of farnesyl diphosphate in tobacco BY-2 cells treated with squalestatin. 2000 Biochem. Soc. Trans. pmid:11171211
Cane DE Cell-free studies of monoterpene and sesquiterpene biosynthesis. 1983 Biochem. Soc. Trans. pmid:6642060
Brindle PA and Threlfall DR The metabolism of phytoalexins. 1983 Biochem. Soc. Trans. pmid:6642061
Parmryd I and Dallner G Organization of isoprenoid biosynthesis. 1996 Biochem. Soc. Trans. pmid:8878825
Reigard SA et al. Interplay of isoprenoid and peptide substrate specificity in protein farnesyltransferase. 2005 Biochemistry pmid:16101305
Micali E et al. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. 2001 Biochemistry pmid:11591144
Dursina B et al. Interaction of yeast Rab geranylgeranyl transferase with its protein and lipid substrates. 2002 Biochemistry pmid:12022885
Holstein SA et al. Isoprenoids influence expression of Ras and Ras-related proteins. 2002 Biochemistry pmid:12427032
Kloer DP et al. Structure and reaction geometry of geranylgeranyl diphosphate synthase from Sinapis alba. 2006 Biochemistry pmid:17176041
Deligeorgopoulou A and Allemann RK Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-beta-farnesene synthase. 2003 Biochemistry pmid:12820883
Roberts MJ et al. Hydrophilic anilinogeranyl diphosphate prenyl analogues are Ras function inhibitors. 2006 Biochemistry pmid:17176109
Turek-Etienne TC et al. Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase. 2003 Biochemistry pmid:12667062
Pan JJ et al. Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. 2000 Biochemistry pmid:10978182
Thomä NH et al. Phosphoisoprenoid binding specificity of geranylgeranyltransferase type II. 2000 Biochemistry pmid:11009619
Radisky ES and Poulter CD Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. 2000 Biochemistry pmid:10677224
Huang C et al. Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state. 2000 Biochemistry pmid:10704208
Long SB et al. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. 1998 Biochemistry pmid:9657673
Subramanian T et al. Farnesyl diphosphate analogues with aryl moieties are efficient alternate substrates for protein farnesyltransferase. 2012 Biochemistry pmid:22989235
Strickland CL et al. Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue. 1998 Biochemistry pmid:9843427
Pompliano DL et al. Steady-state kinetic mechanism of Ras farnesyl:protein transferase. 1992 Biochemistry pmid:1567835
Chang SY et al. Identification of the active conformation and the importance of length of the flexible loop 72-83 in regulating the conformational change of undecaprenyl pyrophosphate synthase. 2003 Biochemistry pmid:14661956
Chen M et al. Mechanistic insights from the binding of substrate and carbocation intermediate analogues to aristolochene synthase. 2013 Biochemistry pmid:23905850
van der Kamp MW et al. Conformational change and ligand binding in the aristolochene synthase catalytic cycle. 2013 Biochemistry pmid:24106830
Butrynski JE et al. Differential isoprenylation of carboxy-terminal mutants of an inhibitory G-protein alpha-subunit: neither farnesylation nor geranylgeranylation is sufficient for membrane attachment. 1992 Biochemistry pmid:1510988
Cane DE et al. Trichodiene synthase. Substrate specificity and inhibition. 1995 Biochemistry pmid:7873526
Cane DE et al. Trichodiene synthase. Identification of active site residues by site-directed mutagenesis. 1995 Biochemistry pmid:7873527
Grundy DJ et al. Mechanism of Germacradien-4-ol Synthase-Controlled Water Capture. 2016 Biochemistry pmid:26998816
Harris GG et al. Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with αα Domain Architecture That Catalyzes a Unique Cyclization-Fragmentation Reaction Sequence. 2015 Biochemistry pmid:26598179
Furfine ES et al. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. 1995 Biochemistry pmid:7756316
Cane DE et al. Trichodiene synthase. Probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis. 1996 Biochemistry pmid:8823172
Omer CA et al. Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. 1993 Biochemistry pmid:8494894
Vogt A et al. Burkitt lymphoma Daudi cells contain two distinct farnesyltransferases with different divalent cation requirements. 1995 Biochemistry pmid:7547984
Cui G and Merz KM Computational studies of the farnesyltransferase ternary complex part II: the conformational activation of farnesyldiphosphate. 2007 Biochemistry pmid:17918965
Dietrich A et al. Isoprenylation of the G protein gamma subunit is both necessary and sufficient for beta gamma dimer-mediated stimulation of phospholipase C. 1996 Biochemistry pmid:8952464
Cane DE et al. Pre-steady-state kinetic analysis of the trichodiene synthase reaction pathway. 1997 Biochemistry pmid:9204880
Mathis JR et al. Pre-steady-state study of recombinant sesquiterpene cyclases. 1997 Biochemistry pmid:9204881
Zhang YW et al. Chain length determination of prenyltransferases: both heteromeric subunits of medium-chain (E)-prenyl diphosphate synthase are involved in the product chain length determination. 2000 Biochemistry pmid:11027152
Shishova EY et al. X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate. 2007 Biochemistry pmid:17261032
Kurth DD et al. Functional consequence of mutating conserved residues of the yeast farnesyl-protein transferase beta-subunit Ram1(Dpr1). 1997 Biochemistry pmid:9398327
Troutman JM et al. Protein farnesyl transferase target selectivity is dependent upon peptide stimulated product release. 2007 Biochemistry pmid:17877368
Troutman JM et al. Selective modification of CaaX peptides with ortho-substituted anilinogeranyl lipids by protein farnesyl transferase: competitive substrates and potent inhibitors from a library of farnesyl diphosphate analogues. 2007 Biochemistry pmid:17854205
Dunten P et al. Protein farnesyltransferase: structure and implications for substrate binding. 1998 Biochemistry pmid:9609683
Fu Z et al. Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism. 2008 Biochemistry pmid:18302342
Keller RK Squalene synthase inhibition alters metabolism of nonsterols in rat liver. 1996 Biochim. Biophys. Acta pmid:8908150
Newman P et al. Polyisoprenylation of the CAAX motif--an in vitro protein synthesis study. 1991 Biochim. Biophys. Acta pmid:1954230
Exnowitz F et al. NMR for direct determination of K(m) and V(max) of enzyme reactions based on the Lambert W function-analysis of progress curves. 2012 Biochim. Biophys. Acta pmid:22079737