Farnesyl pyrophosphate synthase: A key enzyme in isoprenoid biosynthetic pathway and potential molecular target for drug development

New Biotechnology

Volumn 30, Issue 2, 2013, Pages 114-123

  Dhar, Manoj K ^a   Koul, Archana ^a   Kaul, Sanjana ^a  

^a UNIVERSITY OF JAMMU   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHETIC PATHWAY; BISPHOSPHONATES; CELL METABOLISM; CHAIN ELONGATION; DIPHOSPHATES; DRUG DEVELOPMENT; FARNESYL PYROPHOSPHATES; FARNESYLATION; FUNCTIONAL RELATIONSHIP; HUMAN PATHOGENS; ISOPENTENYL DIPHOSPHATE; ISOPRENOIDS; KEY ENZYMES; MOLECULAR TARGETS; SYNTHASES;

BIOCHEMISTRY; BIOSYNTHESIS; ENZYMES; MOLECULAR BIOLOGY; MOLECULAR PHYSICS; PLANTS (BOTANY);

LIPIDS;

ALENDRONIC ACID; GERANYLTRANSFERASE; ISOPRENOID; MEVALONIC ACID; PAMIDRONIC ACID; RISEDRONIC ACID; SHORT HAIRPIN RNA;

DRUG DEVELOPMENT; DRUG SYNTHESIS; DRUG TARGETING; ENZYME ANALYSIS; ENZYME LOCALIZATION; ENZYME STRUCTURE; GANODERMA LUCIDUM; HUMAN; MOLECULAR CLONING; MOLECULAR EVOLUTION; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVIEW; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; BIOSYNTHETIC PATHWAYS; DRUG DISCOVERY; EVOLUTION, MOLECULAR; GERANYLTRANSTRANSFERASE; HUMANS; MOLECULAR SEQUENCE DATA; MOLECULAR TARGETED THERAPY; TERPENES;

EID: 84872380613     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2012.07.001     Document Type: Review

References (100)

1. Poulter C.D. Farnesyl diphosphate synthase. A paradigm for understanding structure and function relationships in E-polyprenyl diphosphate synthases. Phytochem. Rev. 2006, 5:17-26.
2. Lange B.M., et al. Isoprenoid biosynthesis: the evolution of two ancient and distinct pathways across genomes. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:13172-13177.
3. Rohmer, M. et al. (2005) Biosynthetic routes to the building blocks of isoprenoids. Biopolymers Online. Wiley Online Library.
4. Chappell J. Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1995, 46:521-547.
5. Hunter W.N. The non-mevalonate pathway of isoprenoid precursor biosynthesis. J. Biol. Chem. 2007, 282:21573-21577.
6. Lichtenthaler H.K. Non-mevalonate isoprenoid biosynthesis: enzymes, genes and inhibitors. Biochem. Soc. Trans. 2000, 28:785-789.
7. Lombard J., Moreira D. Origins and early evolution of the mevalonate pathway of isoprenoid biosynthesis in the three domains of life. Mol. Biol. Evol. 2010, 28:87-99.
8. Rodriguez-Concepcion M., Boronat A. Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics. Plant Physiol. 2002, 130:1079-1089.
9. Thulasiram H.V., Poulter C.D. Farnesyl diphosphate synthase: the art of compromise between substrate selectivity and stereoselectivity. J. Am. Chem. Soc. 2006, 128:15819-15823.
10. Kellogg B.A., Poulter C.D. Chain elongation in the isoprenoid biosynthetic pathway. Curr. Opin. Chem. Biol. 1997, 1:570-578.
11. Reilly J.F., et al. A novel role for farnesyl pyrophosphate synthase in fibroblast growth factor-mediated signal transduction. Biochem. J. 2002, 366:501-510.
12. Tachibana A., et al. Novel prenyl transferase gene encoding farnesyl geranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity. Eur. J. Biochem. 2000, 267:321-328.
13. Anderson M.S., et al. Farnesyl diphosphate synthetase, molecular cloning, sequence, and expression of an essential gene from Saccharomyces cerevisiae. J. Biol. Chem. 1989, 264:19176-19184.
14. Ding Y.X., et al. Molecular cloning, characterization, and differential expression of a farnesyl diphosphate synthase gene from the basidiomycetous fungus Ganoderma lucidum. Biosci. Biotechnol. Biochem. 2008, 72:1571-1579.
15. Clark C.F., et al. Molecular cloning and sequence of a cholesterol-repressible enzyme related to prenyltransferase in the isoprene biosynthetic pathway. Mol. Cell Biol. 1987, 7:3138-3146.
16. Hemmerlin A., et al. Enzymes encoded by the farnesyl diphosphate synthase gene family in the big sagebrush Artemisia tridentate ssp. spiciformis. J. Biol. Chem. 2003, 278:32132-32140.
17. Attucci S., et al. A cDNA encoding farnesyl pyrophosphate synthase in white lupin. Plant Physiol. 1995, 108:835-836.
18. Matsushita Y., et al. Cloning and analysis of a cDNA encoding farnesyl diphosphate synthase from Artemisia annua. Gene 1996, 172:207-209.
19. Cunillera N., et al. Arabidopsis thaliana contains two differentially expressed farnesyl diphosphate synthase genes. J. Biol. Chem. 1996, 271:7774-7780.
20. Sanmiya K., et al. Cloning of a cDNA that encodes farnesyl diphosphate synthase and the blue light-induced expression of the corresponding gene in the leaves of the rice plants. Biochem. Biophys. Acta 1997, 1350:240-246.
21. Gaffe J., et al. LEFPS1, a tomato farnesyl pyrophosphate gene highly expressed during early fruit development. Plant Physiol. 2000, 123:1351-1362.
22. Mekkriengkrai D., et al. Cloning and characterization of farnesyl diphosphate synthase from the rubber producing mushroom Lactaris chrysorrheus. Biosci. Biotechnol. Biochem. 2004, 68:2360-2368.
23. Cervantes-Cervantes M., et al. Maize cDNA expressed in endosperm encode functional farnesyl diphosphate synthase with geranylgeranyl diphosphate synthase activity. Plant Physiol. 2006, 141:220-231.
24. Liao Z.H., et al. A new farnesyl diphosphate synthase gene from Taxus media Rehder: cloning, characterization and functional complementation. J. Integr. Plant Biol. 2006, 48:692-699.
25. Closa M., et al. The Arabidopsis thaliana FPP synthase isozymes have overlapping and specific functions in isoprenoid biosynthesis, and complete loss of FPP synthase activity causes early developmental arrest. Plant J. 2010, 63:512-525.
26. Gupta P., et al. Differential expression of farnesyl diphosphate synthase gene from Withania somnifera in different chemotypes and in response to elicitors. Plant Growth Regul. 2011, 65:93-100.
27. Castillo-Gracia M., Couillaud F. Molecular cloning and tissue expression of an insect farnesyl diphosphate synthase. Eur. J. Biochem. 1999, 262:365-370.
28. Sheares B.T., et al. Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells. Biochemistry 1989, 28:8129-8135.
29. Wilkin D.J., et al. Isolation and sequence of the human farnesyl pyrophosphate synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methyl glutaryl Coenzyme A reductase, and 3-hydroxy-3-methyl glutaryl Coenzyme A synthase by phorbol ester. J. Biol. Chem. 1990, 265:4607-4614.
30. Montalvetti A., et al. Farnesyl pyrophosphate synthase is an essential enzyme in Trypanosoma brucei. J. Biol. Chem. 2003, 278:17075-17083.
31. Ding V.D., et al. Purification and characterization of recombinant human farnesyl diphosphate synthase expressed in E. coli. Biochem. J. 1991, 275:61-65.
32. Dhiman R.K., et al. Identification of a novel class of omega. E,E-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J. Lipid Res. 2004, 45:1140-1147.
33. Schulbach M.C., et al. Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 2001, 276:11624-11630.
34. Chen A., Poulter C.D. Purification and characterization of farnesyl diphosphate/geranyl geranyl diphosphate synthase. A thermostable bifunctional enzyme from Methanobacterium thermoautotrophicum. J. Biol. Chem. 1993, 268:11002-11007.
35. Barnard G.F., Popjak G. Human liver prenyltransferase and its characterization. Biochem. Biophys. Acta 1981, 661:87-99.
36. Eberhardt N.L., Rilling H.C. Prenyltransferase from Saccharomyces cerevisiae. Purification to homogeneity and molecular properties. J. Biol. Chem. 1975, 250:863-866.
37. Reed B.C., Rilling H.C. Crystallization and partial characterization of prenyltransferase from avian liver. Biochemistry 1975, 14:50-54.
38. Chambon C., et al. Isolation and properties of yeast mutants affected in farnesyl diphosphate synthetase. Curr. Genet. 1990, 18:41-46.
39. Sen S.E., et al. Purification, properties and heteromeric association of type-1 and type-2 lepidopteran farnesyl diphosphate synthases. Insect Biochem. Mol. Biol. 2007, 37:819-828.
40. Okada K., et al. Five geranyl geranyl diphosphate synthases expressed in different organs are localized into three sub cellular compartments in Arabidopsis thaliana. Plant Physiol. 2000, 122:1045-1056.
41. Ortiz-Gomez A., et al. Farnesyl diphosphate synthase is a cytosolic enzyme in Lieshmania major promastigotes and its over expression confers resistance to risedronate. Eukaryot. Cell 2006, 5:1057-1064.
42. Ferella M., et al. Farnesyl diphosphate synthase localizes to the cytoplasm of Trypanosoma cruzi and T. brucei. Exp. Parasitol. 2008, 119:308-312.
43. Liu C.J., et al. Expression pattern of genes encoding farnesyl diphosphate synthase and sesquiterpene cyclase in cotton suspension cultured cells treated with fungal elicitors. Mol. Plant Microbe Interact. 1999, 12:1095-1104.
44. Grunler J., et al. Branch-point reactions in the biosynthesis of cholesterol, dolichol, ubiquinone and prenylated proteins. Biochem. Biophys. Acta 1994, 1212:259-277.
45. Cunillera N., et al. The Arabidopsis thaliana FPS1 gene generates a novel mRNA that encodes a mitochondrial farnesyl diphosphate isoform. J. Biol. Chem. 1997, 272:15381-15388.
46. Runquist M., et al. Isoprenoid biosynthesis in rat liver mitochondria. Studies on farnesyl pyrophosphate synthase and trans-prenyltransferase. J. Biol. Chem. 1994, 269:5804-5809.
47. Zhang Y.L., Li Z.X. Two different farnesyl diphosphate synthase genes exist in the genome of the green peach aphid Myzus persicae. Genome 2008, 51:501-510.
48. Martin D., et al. Mitochondrial targeting of farnesyl diphosphate synthase is a widespread phenomenon in eukaryotes. Biochim. Biophys. Acta 2007, 1773:419-426.
49. Taban A.H., et al. Isolation and characterization of farnesyl diphosphate synthase from the cotton boll weevil, Anthonomus grandis. Insect Biochem. Physiol. 2009, 71:88-104.
50. Krisans S.K., et al. Farnesyl diphosphate synthase is localized in peroxisomes. J. Biol. Chem. 1994, 269:14165-14169.
51. Oliver L.M., Krisans S.K. Peroxisomal protein targeting and identification of the peroxisomal targeting signals in cholesterol biosynthetic enzymes. Biochem. Biophys. Acta 2000, 1529:89-102.
52. Gupta S.D., et al. Differential binding of proteins to peroxisomes in rat hepatoma cells: unique association of enzymes involved in isoprenoid metabolism. J. Lipid Res. 1999, 40:1572-1584.
53. Sanmiya K., et al. Localization of farnesyl diphosphate synthase in chloroplasts. Plant Cell Physiol. 1999, 40:348-354.
54. Daudonnet S., et al. Expression of the farnesyl diphosphate synthase of Saccharomyces cerevisiae in tobacco. Mol. Breed. 1997, 3:137-145.
55. Cusson M., et al. Characterization and tissue-specific expression of two lepidopteran farnesyl diphosphate synthase homologs: implications for the biosynthesis of ethyl-substituted juvenile hormones. Proteins 2006, 65:742-758.
56. Romanelli M.G., et al. Characterization and functional analysis of cis-acting elements of the human farnesyl diphosphate synthetase (FDPS) gene 5' flanking region. Genomics 2008, 93:227-234.
57. Ling Y., et al. The farnesyl-diphosphate/geranylgeranyl-diphosphate synthase of Toxoplasma gondii is a bifunctional enzyme and a molecular target of bisphosphonates. J. Biol. Chem. 2007, 282:30804-30816.
58. Tarshis L.C., et al. Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-å resolution. Biochemistry 1994, 33:10871-10877.
59. Hosfield D.J., et al. Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis. J. Biol. Chem. 2004, 279:8526-8529.
60. Ashby M.N., Edwards P.A. Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase. J. Biol. Chem. 1990, 265:13157-13164.
61. Koyama T., et al. Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification. J. Biochem. 1993, 113:355-363.
62. Szkopinska A., Plochocka D. Farnesyl diphosphate synthase; regulation of product specificity. Acta Biochim. Pol. 2005, 52:45-55.
63. Tarshis L.C., et al. Regulation of product chain length by isoprenyl diphosphate synthases. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:15018-15023.
64. Ohnuma S., et al. Conversion from farnesyl diphosphate synthase to geranyl geranyl diphosphate synthase by random chemical mutagenesis. J. Biol. Chem. 1999, 271:10087-10095.
65. Koyama T., et al. Identification of significant residues in the substrate binding site of Bacillus stearothermophilus farnesyl diphosphate synthase. Biochemistry 1996, 35:9533-9538.
66. Song L., Poulter C.D. Yeast farnesyl diphosphate synthase: site directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Proc. Natl. Acad. Sci. U. S. A. 1994, 19:3044-3048.
67. Ohnuma S., et al. A role of the amino acid residue located on the fifth position before the first Aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product. J. Biol. Chem. 1996, 271:30748-30754.
68. Ohnuma S., et al. Conversion of product specificity of archaebacterial geranyl geranyl diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyltransferase reaction. J. Biol. Chem. 1996, 271:18831-18832.
69. Ohnuma S., et al. A pathway where polyprenyl diphosphate elongates in prenyltransferase. Insight into a common mechanism of chain length determination of prenyltransferases. J. Biol. Chem. 1998, 273:26705-26713.
70. Narita K., et al. Protein design of geranyl diphosphate synthase. Structural features that define the product specificities of prenyltransferase. J. Biochem. 1999, 126:566-571.
71. Fischer M.J.C., et al. Identification of a lysine residue important for the catalytic activity of yeast farnesyl diphosphate synthase. Protein J. 2011, 30:334-339.
72. James M.N.G., et al. Amino acid sequence alignment of bacterial and mammalian pancreatic serine proteases based on topological equivalences. Can. J. Biochem. 1978, 56:396-402.
73. Bajaj M., Blundell T. Evolution and the tertiary structure of proteins. Annu. Rev. Biophys. Bioeng. 1984, 13:453-492.
74. Clothia C., Lesk A.M. The relation between the divergence of sequence and structure in proteins. EMBO J. 1986, 5:823-826.
75. Chen A., et al. Isoprenyl diphosphate synthases: protein sequence comparison, a phylogenetic tree, and predictions of secondary structure. Protein Sci. 1994, 3:600-607.
76. Lee P.C., et al. Alteration of product specificity of Aeropyrum pernix farnesyl geranyl diphosphate synthase (Fgs) by site directed evolution. Protein Eng. Des. Sel. 2004, 17:771-777.
77. Ohnuma S., et al. Conversion from archeal geranyl geranyl synthase to farnesyl diphosphate synthase. Two amino acid before the first Aspartate rich motif solely determine eukaryotic farnesyl diphosphate synthase activity. J. Biol. Chem. 1997, 272:5192-5198.
78. Fleisch H. Bisphosphonates. Pharmacology and use in the treatment of tumor induced hypercalcaemic and metastatic bone disease. Drugs 1991, 42:919-944.
79. Lahtinen R., et al. Randomized, placebo-controlled multicentre trail of clodronate in multiple myeloma. Lancet 1992, 34:1049-1052.
80. Shipman C.M., et al. Bisphosphonate induces apoptosis in human myeloma cell lines. Br. J. Haematol. 1997, 98:665-672.
81. Smith R., et al. Diphosphonates and Paget's disease of bone. Lancet 1971, 1:945-947.
82. Rodan G.A. Mechanism of action of bisphosphonates. Ann. Rev. Pharmacol. Toxicol. 1998, 38:375-388.
83. Brown D.L., Robbins R. Developments in the therapeutic applications of bisphosphonates. J. Clin. Pharmacol. 1999, 39:651-660.
84. Rodan G.A., Martin T.J. Therapeutic approaches to bone diseases. Science 2000, 289:1508-1514.
85. Levy J., Roodman G.D. The role of bisphosphonate in mutilpe myeloma. Curr. Hematol. Malig. Rep. 2009, 4:108-112.
86. Beek E.V., et al. Farnesyl pyrophosphate synthase is the molecular target of nitrogen-containing bisphosphonates. Biochem. Biophys. Res. Commun. 1999, 264:108-111.
87. Cromartie T.H., et al. The discovery of a novel site of action for herbicidal bisphosphonates. Pestic. Physiol. Biochem. 1999, 63:114-126.
88. Martin M.B., et al. Nitrogen-containing bisphosphonates as carbocation transition state analogs for isoprenoid biosynthesis. Biochem. Biophys. Res. Commun. 1999, 263:754-758.
89. Grove J.E., et al. The intracellular target for the antiresorptive amino bisphosphonate drugs in Dictyostelium discoideum is the enzyme farnesyl pyrophosphate synthase. J. Bone Miner. Res. 2000, 15:971-981.
90. Dunford J.E., et al. Structure-activity relationships for inhibition of farnesyl pyrophosphate synthase in vitro and inhibition of bone resorption in vivo by nitrogen containing bisphosphonates. J. Pharmacol. Exp. Ther. 2001, 296:235-242.
91. Raikkonen J., et al. Correlation between time-dependent inhibition of human farnesyl pyrophosphate synthase and blockade of mevalonate pathway by nitrogen-containing bisphosphonate in cultured cells. Biochem. Biophys. Res. Commun. 2011, 407:663-667.
92. Yardley V., et al. In vivo activities of farnesyl pyrophosphate synthase inhibitors against Lieshmania donovani and Toxoplasma gondii. Antimicrob. Agents Chemother. 2002, 46:929-931.
93. Szajnman S.H., et al. Synthesis and biological evolution of 1-amino-1,1-bisphosphonates derived from fatty acids against Trypanosoma cruzi targeting farnesyl pyrophosphate synthase. Bioorg. Med. Chem. Lett. 2005, 15:4685-4690.
94. Eubank W.B., Reeves R.E. Analog inhibitors for the pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica and their effect on culture growth. J. Parasitol. 1982, 68:599-602.
95. Jackson N.M., Kocarek T.A. Suppression of CYP2B induction by alendronate-mediated farnesyl diphosphate synthase inhibition in primary cultured rat hepatocytes. Drug Metab. Dispos. 2008, 36:2030-2036.
96. Mukkamala D., et al. Bisphosphonate inhibition of a plasmodium farnesyl diphosphate synthase and a general method for predicting cell based activity from enzyme data. J. Med. Chem. 2008, 51:7827-7833.
97. Gabelli S.B., et al. Structure and mechanism of the farnesyl diphosphate synthase from Trypanosoma cruzi: implications for drug design. Proteins 2006, 62:80-88.
98. Notarnicola M., et al. Higher farnesyl diphosphate synthase activity in human colorectal cancer: inhibition of cellular apoptosis. Oncology 2004, 67:351-358.
99. Li J., et al. Reduced expression of the mevalonate pathway enzyme farnesyl pyrophosphate synthase unveils recognition of tumor cells by Vγ9Vδ2T cells. J. Immunol. 2009, 182:8118-8124.
100. Oldfield E. Targeting isoprenoid biosynthesis for drug discovery: bench to bedside. Acc. Chem. Res. 2010, 43:1216-1226.