Biosynthetic Routes Diverting from Intermediates of Isoprenoid Biosynthesis to Related Products of the Metabolism
Part 2. Polyisoprenoids
Dr. Yuan-Wei Zhang,
Prof.Dr. Tanetoshi Koyama,
Dr. Yuan-Wei Zhang
- [email protected]
- +81-22-217-5623 | Fax: +81-22-217-5620
Tohoku University, Institute of Multidisciplinary Research for Advanced Materials, Katahira 2-1-1, Aoba-ku, Sendai, Japan, 980–8577
Search for more papers by this authorProf.Dr. Tanetoshi Koyama
- [email protected]
- +81-22-217-5621 | Fax: +81-22-217-5620
Tohoku University, Institute of Multidisciplinary Research for Advanced Materials, Katahira 2-1-1, Aoba-ku, Sendai, Japan, 980–8577
Search for more papers by this authorDr. Yuan-Wei Zhang,
Prof.Dr. Tanetoshi Koyama,
Dr. Yuan-Wei Zhang
- [email protected]
- +81-22-217-5623 | Fax: +81-22-217-5620
Tohoku University, Institute of Multidisciplinary Research for Advanced Materials, Katahira 2-1-1, Aoba-ku, Sendai, Japan, 980–8577
Search for more papers by this authorProf.Dr. Tanetoshi Koyama
- [email protected]
- +81-22-217-5621 | Fax: +81-22-217-5620
Tohoku University, Institute of Multidisciplinary Research for Advanced Materials, Katahira 2-1-1, Aoba-ku, Sendai, Japan, 980–8577
Search for more papers by this authorAbstract
- Introduction
- History
- Structural Determination
- Biosynthesis of Isoprenoid Compounds
- Biosynthesis Routes of Polyisoprenoid Compounds
- Squalene and Triterpenes
- General Introduction
- Biosynthesis of Squalene and Plant Triterpenes
- Steroids
- General Introduction
- Cholesterol Biosynthesis
- Ergosterol Biosynthesis
- Biosynthesis of Higher Plant Sterols
- Biosynthesis of Bile Acid
- Biosynthesis of Human Sex Hormones
- Carotenoids
- General Introduction
- Biosynthetic Pathway
- Ubiquinones and Menaquinones
- General Introduction
- Coenzyme Q Biosynthesis
- Menaquinone Biosynthesis
- Dolichols and Related Compounds
- General Introduction
- Biosynthesis of Polyprenyl Diphosphates
- Biosynthesis of End Products
- Squalene and Triterpenes
- Future Prospects
- Acknowledgements
References
- Abe, I., Prestwich, G. D. (1995) Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA, Proc. Natl. Acad. Sci. USA 92, 9274–9278.
-
Abe, I.,
Prestwich, G. D.
(1999)
Squalene epoxidase and oxidosqualene:lanosterol cyclase – key enzymes in cholesterol biosynthesis, in: Comprehensive Natural Products Chemistry, Vol. 2 ( S. D. Barton, K. Nakanishi, O. Meth-Cohn, Eds.), pp. 267–298. Oxford: Elsevier.
10.1016/B978-0-08-091283-7.00045-X Google Scholar
- Abe, I., Ebizuka, Y., Sankawa, U. (1988) Purification of 2,3-oxidosqualene:cycloartenol cyclase from pea seedlings, Chem. Pharm. Bull. 36, 5031–5034.
- Abe, I., Ebizuka, Y., Sankawa, U. (1989a) Purification of squalene-2,3-epoxide cyclases from cell suspension cultures of Rabdosia japonica Hara, FEBS Lett. 249, 100–104.
- Abe, I., Sankawa, U., Ebizuka, Y. (1989b) Purification of 2,3-oxidosqualene:β-amyrin cyclase from pea seedlings, Chem Pharm. Bull. 37, 536–538.
- Abe, I., Rohmer, M., Prestwich, G. D. (1993) Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpene, Chem. Rev. 93, 2189–2206.
- Adair, W. L., Jr., Cafmeyer, N. (1987) Characterization of the Saccharomyces cerevisiae cis-prenyltransferase required for dolichyl phosphate biosynthesis, Arch. Biochem. Biophys. 259, 589–596.
- Alexander, K., Young, I. G. (1978) Alternative hydroxylases for the aerobic and anaerobic biosynthesis of ubiquinone in Escherichia coli, Biochemistry 17, 4750–4755.
- Allen, C. M., Jr., Kalin, J. R., Sack, J., Verizzo, D. (1978) CTP-dependent dolichol phosphorylation by mammalian cell homogenates, Biochemistry 17, 5020–5026.
- Altman, L. J., Kowerski, R. C., Launganni, D. R. (1978) Studies in terpene biosynthesis. Synthesis and resolution of presqualene and prephytoene alcohols, J. Am. Chem. Soc. 100, 6174–6182.
- Aoyama, Y., Yoshida, Y., Sato, R. (1984) Yeast cytochrome P-450 catalyzing lanosterol 14-α-demethylation. II. Lanosterol metabolism by purified P-450 (14) DM and by intact microsomes, J. Biol. Chem. 259, 1661–1666.
- Apfel, C. M., Takacs, B., Fountoulakis, M., Stieger, M., Keck, W. (1999) Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene, J. Bacteriol. 181, 483–492.
-
Armstrong, G. A.
(1999)
Carotenoid genetics and biochemistry, in: Comprehensive Natural Products Chemistry, Vol. 2 ( S. D. Barton, K. Nakanishi, O. Meth-Cohn, Eds.), pp. 321–352. Oxford: Elsevier.
10.1016/B978-0-08-091283-7.00047-3 Google Scholar
- Armstrong, G. A., Hearst, J. E. (1996) Genetics and molecular biology of carotenoid pigment biosynthesis, FASEB J. 10, 228–237.
- Armstrong, G. A., Alberti, M., Hearst, J. E. (1990) Conserved enzymes mediate the early reactions of carotenoid biosynthesis in nonphotosynthetic and photosynthetic prokaryotes, Proc. Natl. Acad. Sci. USA 87, 9975–9979.
- Asai, K., Fujisaki, S., Nishimura, Y., Nishino, T., Okada, K. et al. (1994) The identification of Escherichia coli ispB (cel) gene encoding the octaprenyl diphosphate synthase, Biochem. Biophys. Res. Commun. 202, 340–345.
- Ashby, M. N., Kutsunai, S. Y., Ackerman, S., Tzagoloff, A., Edwards, P. A. (1992) COQ2 is a candidate for the structural gene encoding p-hydroxybenzoate:polyprenyltransferase, J. Biol. Chem. 267, 4128–4136.
- Astrand, I. M., Fries, E., Chojnacki, T., Dallner, G. (1986 ) Inhibition of dolichyl phosphate biosynthesis by compactin in cultured rat hepatocytes, Eur. J. Biochem. 155, 447–452.
- Baba, T., Allen, C. M., Jr. (1978) Substrate specificity of undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum, Biochemistry 17, 5598–5604.
- Bach, T. J., Benveniste, P. (1997) Cloning of cDNAs or genes encoding enzymes of sterol biosynthesis from plants and other eukaryotes: heterologous expression and complementation analysis of mutations for functional characterization, Prog. Lipid Res. 36, 197–226.
- Bae, S. H., Paik, Y. K. (1997) Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol Δ24-reductase, Biochem. J. 326, 609–616.
- Baker, C. H., Matsuda, S. P., Liu, D. R., Corey, E. J. (1995) Molecular cloning of the human gene encoding lanosterol synthase from a liver cDNA library, Biochem. Biophys. Res. Commun. 213, 154–160.
- Baldwin, B. C. (1990) Inhibitors of ergosterol biosynthesis as crop protection agents, Biochem. Soc. Trans. 18, 61–62.
- Bartley, G. E., Viitanen, P. V., Bacot, K. O., Scolnik, P. A. (1992) A tomato gene expressed during fruit ripening encodes an enzyme of the carotenoid biosynthesis pathway, J. Biol. Chem. 267, 5036–5039.
- Bartsch, W., Greeve, J., Voigt, K. D. (1987) 17 β-Hydroxysteroid dehydrogenase in the human prostate: properties and distribution between epithelium and stroma in benign hyperplastic tissue, J. Steroid Biochem. 28, 35–42.
- Bartsch, W., Klein, H., Schiemann, U., Bauer, H. W., Voigt, K. D. (1990) Enzymes of androgen formation and degradation in the human prostate, Ann. N. Y. Acad. Sci. 595, 53–66.
- Benveniste, P. (1986) Sterol biosynthesis, Annu. Rev. Plant Physiol. 37, 275–308.
- Bouvier, F., Hugueney, P., d'Harlingue, A., Kantz, M., Camara, B. (1994) Xanthophyll biosynthesis in chromoplasts: isolation and molecular cloning of an enzyme catalyzing the conversion of 5,6-epoxycarotenoid into ketocarotenoid, Plant J. 6, 45–54.
- Bradshaw, K. D., Waterman, M. R., Couch, R. T., Simpson, E. R., Zuber, M. X. (1987) Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 α-hydroxylase: a probe for analysis of 17 α-hydroxylase deficiency, Mol. Endocrinol. 1, 348–354.
- Britton, G. (1995) Structure and properties of carotenoids in relation and function, FASEB J. 9, 1551–1558.
- Bryant, R. W., Jr., Bentley, R. (1976) Menaquinone biosynthesis: conversion of O-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid and menaquinones by Escherichia coli extracts, Biochemistry 15, 4792–4796.
- Bukhtiyarov, Y. E., Shabalin, Y. A., Kulaev, I. S. (1993) Solubilization and characterization of dehydrodolichyl diphosphate synthase from the yeast Saccharomyces carlsbergensis, J. Biochem. (Tokyo) 113, 721–728.
- Burgos, J., Hemming, F. W., Pennock, J. F., Morton, R. A. (1963) Dolichol: a naturally occurring C100 isoprenoid alcohol, Biochem. J. 88, 470–482.
- Butenandt, A. (1931) Chemical investigation of the sex hormones, Z. Angew. Chem. 44, 905–908.
- Cali, J. J., Russell, D. W. (1991) Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis, J. Biol. Chem. 266, 7774–7778.
- Camara, B., Bardat, F., Moneger, R. (1982) Sites of biosynthesis of carotenoids in Capsicum chromoplasts, Eur. J. Biochem. 127, 255–258.
-
Campbell, I. M.
(1969)
The roles of alanine, aspartate and glutamate in lawsone biosynthesis in Impatiens balsamina,
Tetrahedron Lett. 1969,
4777–4780.
10.1016/S0040-4039(01)88807-9 Google Scholar
- Cane, D. E. (1990) Enzymatic formation of sesquiterpenes, Chem. Rev. 90, 1089–1103.
- Carroll, K. K., Guthrie, N., Ravi, K. (1992) Dolichol: function, metabolism, and accumulation in human tissues, Biochem. Cell Biol. 70, 382–384.
- Chamovitz, D., Misawa, N., Sandmann, G., Hirschberg, J. (1992) Molecular cloning and expression in Escherichia coli of a cyanobacterial gene coding for phytoene synthase, a carotenoid biosynthesis enzyme, FEBS Lett. 296, 305–310.
- Chaykin, S., Law, J., Phillips, A. H., Tehen, T. T., Bloch, K. (1958) Phosphorylated intermediates in the synthesis of squalene, Proc. Natl. Acad. Sci. USA 44, 998–1004.
- Choi, Y. L., Nishida, T., Kawamukai, M., Utsumi, R., Saka, H., Komano, T. (1989) Cloning and sequencing of an Escherichia coli gene, nlp, highly homologous to the ner genes of bacteriophages Mu and D108, J. Bacteriol. 171, 5222–5225.
- Chojnacki, T., Vogtman, T. (1984) The occurrence and seasonal distribution of C50–C60-polyprenols and of C100 and similar long-chain polyprenols in leaves of plants, Acta Biochim. Pol. 31, 115–126.
- Clayton, R. B., Bloch, K. (1956) Biological synthesis of lanosterol and agnosterol, J. Biol. Chem. 218, 305–318.
- Corey, E. J., Volante, R. P. (1976) Application of unreactive analogs of terpenoid pyrophosphates to studies of multistep biosynthesis. Demonstration that “presqualene pyrophosphate” is an essential intermediate on the path to squalene, J. Am. Chem. Soc. 98, 1291–1293.
- Corey, E. J., Virgil, S. C., Sarshar, S. (1991) An experimental demonstration of the stereochemistry of enzymic cyclization of 2,3-oxidosqualene to the protosterol system, forerunner of lanosterol and cholesterol, J. Am. Chem. Soc. 113, 4025–4027.
- Corey, E. J., Matsuda, S. P., Bartel, B. (1993) Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen, Proc. Natl. Acad. Sci. USA 90, 11628–11632.
- Corey, E. J., Matsuda, S. P., Bartel, B. (1994) Molecular cloning, characterization, and overexpression of ERG7, the Saccharomyces cerevisiae gene encoding lanosterol synthase, Proc. Natl. Acad. Sci. USA 91, 2211–2215.
- Cox, G. B., Young, I. G., McCann, L. M., Gibson, F. (1969) Biosynthesis of ubiquinone in Escherichia coli K-12: location of genes affecting the metabolism of 3-octaprenyl-4-hydroxybenzoic acid and 2-octaprenylphenol, J. Bacteriol. 99, 450–458.
- Crane, F. L. (1977) Hydroquinone dehydrogenases, Annu. Rev. Biochem. 46, 439–469.
- Croteau, R. (1987) Biosynthesis and catabolism of monoterpenoids, Chem. Rev. 87, 929–954.
- Croteau, R. (1998) Plant terpenoid synthases: Molecular biology and phylogenetic analysis, Proc. Natl. Acad. Sci. USA 45, 4126–4133.
- Dahlbach, H., Holmberg, I. (1990) Oxidation of 5β-cholestane-3α,7α,12α-triol into 3α,7α,12α-trihydroxy-5β-cholestanoic acid by cytochrome P-450(26) from rabbit liver mitochondria, Biochem. Biophys. Res. Commun. 167, 391–395.
- Dewick, P. M. (1997) The biosynthesis of C5–C25 terpenoid compounds, Nat. Prod. Rep. 14, 111–144.
- Do, T. Q., Schultz, J. R. Clarke, C. F. (1996) Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids, Proc. Natl. Acad. Sci. USA 93, 7534–7539.
- Dogbo, O., Laferrere, A., d'Harlingue, A., Camara, B. (1988) Carotenoid biosynthesis: isolation and characterization of a bifunctional enzyme catalyzing the synthesis of phytoene, Proc. Natl. Acad. Sci. USA 85, 7054–7058.
- Dougherty, D. A. (1996) Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp, Science 271, 163–168.
- Eggens, I., Chojnacki, T., Kenne, L., Dallner, G. (1983) Separation, quantitation and distribution of dolichol and dolichyl phosphate in rat and human tissues, Biochim. Biophys. Acta 751, 355–368.
- Eisenreich, W., Mwnhard, B., Hylands, P. J., Zenk, M. H., Bacher, A. (1996) Studies on the biosynthesis of taxol: the taxane carbon skeleton is not of mevalonoid origin, Proc. Natl. Acad. Sci. USA 93, 6431–6436.
- Ekstroem, T. J., Chojnacki, T., Dallner, G. (1987a) The α-saturation and terminal events in dolichol biosynthesis, J. Biol. Chem. 262, 4090–4097.
- Ekstroem, T. J., Ericssion, J., Dallner, G. (1987b) Localization and terminal reactions of dolichol biosynthesis, Chem. Scr. 27, 39–47.
- Farrants, A. K. O., Bjorkhem, I., Pedersen, J. I. (1989) Identification of 3α,7α,12α-trihydroxy-5β-cholest-24-enoic acid as an intermediate in the peroxisomal conversion of 3α,7α,12α-trihydroxy-5β-cholestanoic acid to cholic acid, Biochim. Biophys. Acta 1002, 198–202.
- Fears, R. (1981) The contribution of the cholesterol biosynthetic pathway to intermediary metabolism and cell function, Biochem. J. 199, 1–7.
- Fonteneau, P., Hartmann-Bouillon, M. A., Benveniste, P. (1977) A 24-methylene lophenol C-28 methyltransferase from suspension cultures of bramble cells, Plant Sci. Lett. 10, 147–155.
- Fujisaki, S., Nishino, T., Katsuki, H. (1986) Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis, J. Biochem. (Tokyo) 99, 1327–1337.
- Fujisaki, S., Hara, H., Nishimura, Y., Horiuchi, K., Nishino, T. (1990) Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli, J. Biochem. (Tokyo) 108, 995–1000.
- Gaylor, J. L. (1981) Formation of sterols in animals, in: Biosynthesis of Isoprenoid Compounds, Vol. 1 ( J. W. Porter, S. L. Spurgeon, Eds.), pp. 481–543. New York: John Wiley & Sons.
- Gaylor, J. L., Delwiche, C. V., Swindell, A. C. (1966) Enzymatic isomerization (Δ8→Δ7) of intermediates of sterol, Steroids 8, 353–363.
- Gibson, F. (1973) Chemical and genetic studies on the biosynthesis of ubiquinone by Escherichia coli, Biochem. Soc. Trans. 1, 317–326.
- Goad, L. J., Goodwin, T.W. (1972) Biosynthesis of plant sterols, Progr. Phytochem. 3, 113–198.
- Goad, L. J., Lenton, J. R., Knapp, F. F., Goodwin, T. W. (1974) Phytosterol side chain biosynthesis, Lipids 9, 582–595.
- Goodwin, T. W. (1979) Biosynthesis of terpenoids, Annu. Rev. Plant Physiol. 30, 369–404.
- Gough, D. P., Kirby, A. L., Richards, J. B., Hemming, F. W. (1970) The characterization of undecaprenol of Lactobacillus plantarum, Biochem. J. 118, 167–170.
- Grinstead, G. F., Gaylor, J. L. (1982) Total enzymic synthesis of cholesterol from 4,4,14 α-trimethyl-5-α-cholesta-8,24-dien-3β-ol. Solubilization, resolution, and reconstitution of Δ 7-sterol 5-desaturase, J. Biol. Chem. 257, 13937–13944.
- Grob, E. C., Kirschner, K., Lynen, F. (1961) Recent information on the biosynthesis of carotenoids, Chimia 15, 308–310.
- Hanley, K. M., Nicolas, O., Donaldson, T. B., Smith-Monroy, C., Robinson, G. W., Hellmann, G. M. (1996) Molecular cloning, in vitro expression and characterization of a plant squalene synthetase cDNA, Plant Mol. Biol. 30, 1139–1151.
- Haslewood, G. A. (1967) Bile salt evolution, J. Lipid Res. 8, 535–550.
- Hata, S., Nishino, T., Komori, M., Katsuki, H. (1981) Involvement of cytochrome P-450 in Δ22-desaturation in ergosterol biosynthesis of yeast, Biochem. Biophys. Res. Commun. 103, 272–277.
- Hemming, F. W. (1983) The biosynthesis of polyisoprenoid chains, Biochem. Soc. Trans. 11, 497–504.
- Higashi, Y., Strominger, J. L., Sweelek, C. C. (1967) Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol, Proc. Natl. Acad. Sci. USA 57, 1878–1884.
- Hui, D. Y. (1996) Molecular biology of enzymes involved with cholesterol ester hydrolysis in mammalian tissues, Biochim. Biophys. Acta 1303, 1–14.
- Ishii, K., Sagami, H., Ogura, K. (1985) Decaprenyl pyrophosphate synthetase from Paracoccus denitrificans, Biochim. Biophys. Acta 835, 291–297.
- Ito, M., Kobayashi, M., Koyama, T., Ogura, K. (1987) Stereochemical analysis of prenyltransferase reactions leading to (Z)- and (E)-polyprenyl chains, Biochemistry 26, 4745–4750.
- IUPAC-IUB Commission on Biochemical Nomenclature. (1965) Tentative rules. nomenclature of quinones with isoprenoid side-chains, Biochim. Biophys. Acta 107, 5–10.
- Jackman, L. M., O'Bien, I. G., Cox, G. B., Gibson, F. (1967) Methionine as the source of methyl groups for ubiquinone and vitamin K: a study using nuclear magnetic resonance and mass spectrometry, Biochim. Biophys. Acta 141, 1–7.
- Jennings, S. M., Tsay, Y. H., Fisch, T. M., Robinson, G. W. (1991) Molecular cloning and characterization of the yeast gene for squalene synthetase, Proc. Natl. Acad. Sci. USA 88, 6038–6042.
- Jeong, J. H., Kitakawa, M., Isono, S., Isono, K. (1993) Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli, DNA Seq. 4, 59–67.
- Jones, H., Rasmusson, G. H. (1980) Recent advances in the biology and chemistry of vitamin D, Fortschr. Chem. Org. Naturst. 39, 63–121.
- Kagan, V., Serbinova, E., Packer, L. (1990) Antioxidant effects of ubiquinones in microsomes and mitochondria are mediated by tocopherol recycling, Biochem. Biophys. Res. Commun. 169, 851–857.
- Karrer, P., Helfenstein, A. (1931) Synthese des Squalens, Helv. Chim. Acta 14, 78–85.
- Karrer, P., Helfenstein, A., Wehrli, H., Wettstein, A. (1930) Pflanzenfarbstoffe (XXV). Über die Konstitution des Lycopins und Carotins, Helv. Chim. Acta 13, 1084–1099.
- Kawata, S., Trzaskos, J. M., Gaylor, J. L. (1985) Microsomal enzymes of cholesterol biosynthesis from lanosterol. Purification and characterization of Δ7-sterol 5-desaturase of rat liver microsomes, J. Biol. Chem. 260, 6609–6617.
- Keller, R. K., Adair, W. L., Jr. (1977) Microdetermination of dolichol in tissues, Biochim. Biophys. Acta 489, 330–336.
- Koike-Takeshita, A., Koyama, T., Ogura, K. (1997) Identification of a novel gene cluster participating in menaquinone (vitamin K2) biosynthesis. Cloning and sequence determination of the 2-heptaprenyl-1,4-naphthoquinone methyltransferase gene of Bacillus stearothermophilus, J. Biol. Chem. 272, 12380–12383.
- Koyama, T., Kokubun, T., Ogura, K. (1988) Polyprenyl diphosphate synthase from mulberry leave: stereochemistry of hydrogen elimination in the prenyltransferase reaction, Photochemistry 27, 2005–2009.
- Koyama, T., Obata, S., Osabe, M., Takeshita, A., Yokoyama, K. et al. (1993) Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification, J. Biochem. 113, 355–363.
- Kurokawa, T., Ogura, K., Seto, S. (1971) Formation of polyprenyl phosphates by a cell-free enzyme of Micrococcus lysodeikticus, Biochem. Biophys. Res. Commun. 45, 251–257.
- Kusano, M., Abe, I., Sankawa, U., Ebizuka, Y. (1991) Purification and some properties of squalene-2,3-epoxide: lanosterol cyclase from rat liver, Chem. Pharm. Bull. 39, 239–241.
- Kuswik-Rabiega, G., Rilling, H. C. (1987) Squalene synthetase. Solubilization and partial purification of squalene synthetase, copurification of presqualene pyrophosphate and squalene synthetase activities, J. Biol. Chem. 262, 1505–1509.
- Lavie, D., Glotter, E. (1971) The cucurbitanes, a group of tetracyclic triterpenes, Fortschr. Chem. Org. Naturst. 29, 307–362.
- Lawrence, J., Cox, G. B., Gibson, F. (1974) Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate, J. Bacteriol. 118, 41–45.
- Lees, N. D., Skaggs, B., Kirsch, D. R., Bard, M. (1995) Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae, Lipids 30, 221–226.
- Li, Y. C., Wang, D. P., Chiang, J. Y. (1990) Regulation of cholesterol 7α-hydroxylase in the liver. Cloning, sequencing, and regulation of cholesterol 7α-hydroxylase mRNA, J. Biol. Chem. 265, 12012–12019.
- Lorence, M. C., Murry, B. A., Trant, J. M., Mason, J. I. (1990) Human 3β-hydroxysteroid dehydrogenase/Δ5→4 isomerase from placenta: expression in nonsteroidogenic cells of a protein that catalyzes the dehydrogenation/isomerization of C21 and C19 steroids, Endocrinology 126, 2493–2498.
- Low, P., Dallner, G., Mayor, S., Cohen, S., Chait, B. T., Menon, A. K. (1991) The mevalonate pathway in the bloodstream form of Trypanosoma brucei. Identification of dolichols containing 11 and 12 isoprene residues, J. Biol. Chem. 266, 19250–19257.
- Loza-Tavera, H. (1999) Monoterpenes in essential oils: Biosynthesis and properties, Adv. Exp. Med. Biol. 464, 49–62.
- Lynen, F., Eggerer, H., Henning, U., Kessel, I. (1958) Farnesyl-pyrophosphat und 3-Methyl-Δ3-butenyl-1-pyrophosphat, die biologischen Vorstufen des Squalens, Angew. Chem. 70, 738–742.
- Lynen, F., Agranoff, B. W., Eggerer, H., Henning, U., Moslein, E. M. (1959) α,α-Dimethyl-allyl-pyrophosphat und Geranyl-pyrophosphat, biologische Vorstufen des Squalens, Angew. Chem. 71, 657–663.
- Mankowski, T., Sasak, W., Janczura, E., Chojnacki, T. (1977) Specificity of polyprenyl phosphates in the in vitro formation of lipid-linked sugars, Arch. Biochem. Biophys. 181, 393–401.
- Matsuoka, S., Sagami, H., Kurisaki, A., Ogura, K. (1991) Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver, J. Biol. Chem. 266, 3464–3468.
- McKenzie, T. L., Jiang, G., Straubhaar, J. R., Conrad, D. G., Shechter, I. (1992) Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase, J. Biol. Chem. 267, 21368–21374.
- Meganathan, R., Bentley, R. (1983) Thiamine pyrophosphate requirement for O-succinylbenzoic acid synthesis in Escherichia coli and evidence for an intermediate, J. Bacteriol. 153, 739–746.
- Mercer, E. I. (1993) Inhibitors of sterol biosynthesis and their applications, Prog. Lipid Res. 32, 357–416.
- Miller, W. L., Gaylor, J. L. (1970) Investigation of the component reactions of oxidative sterol demethylation. Oxidation of a 4α-methyl sterol to a 4α-carboxylic acid during cholesterol biosynthesis, J. Biol. Chem. 245, 5369–5374.
- Mulheira, L. J., Ramm, P. J. (1972) The biosynthesis of sterols, Chem. Soc. Res. 1, 259–291.
- Muscio, F., Carlson, J. P., Kuehl, L., Rilling, H. C. (1974) Presqualene pyrophosphate. A normal intermediate in squalene biosynthesis, J. Biol. Chem. 249, 3746–3749.
- Nakamura, M., Sato, R. (1979) The roles of soluble factors in squalene epoxidation by rat liver microsomes, Biochem. Biophys. Res. Commun. 89, 900–906.
- Nakanishi, K. (1974) Steroids, in: Natural Products Chemistry, Vol. 1 ( K. Nakanishi, T. Goto, S. Ito, S. Natori, S. Nozoe, Eds.), pp. 421–545. Tokyo: Kodansha.
- Nakashima, T., Inoue, T., Oka, A., Nishino, T., Osumi, T., Hata, S. (1995) Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase, Proc. Natl. Acad. Sci. USA 92, 2328–2332.
- Nes, W. D., Janssen, G. G., Bergenstrahle, A. (1991) Structural requirements for transformation of substrates by the (S)-adenosyl-l-methionine: Δ24(25)-sterol methyl transferase, J. Biol. Chem. 266, 15202–15212.
- Newton, N. A., Cox, G. B., Gibson, F. (1971) The function of menaquinone (vitamin K2) in Escherichia coli K-12, Biochim. Biophys. Acta 244, 155–166.
- Noshiro, M., Nishimoto, M., Morohashi, K., Okuda, K. (1989) Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression, FEBS Lett. 257, 97–100.
- Ogura, K., Koyama, T. (1998) Enzymatic aspects of isoprenoid chain elongation, Chem. Rev. 98, 1263–1276.
- Ohnuma, S., Koyama, T., Ogura, K. (1991) Purification of solanesyl-diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase, J. Biol. Chem. 266, 23706–23713.
- Okuda, K., Takigawa, N., Fukuba, R., Kuwaki, T. (1969) 5β-cholestane-3α,7α,12α, 26-tetrol:NAD+ oxidoreductase and 5β-cholestane-3α,7α,12α-triol-26-al:NAD+ oxidoreductase in rat liver, Biochim. Biophys. Acta 185, 1–8.
- Ono, T., Takahashi, K., Odami, S., Konno, H., Imai, Y. (1980) Purification of squalene epoxidase from rat liver microsomes, Biochem. Biophys. Res. Commun. 96, 522–528.
- Ourisson, G., Rohmer, M. (1992) Hopanoids. 2. Biohopanoids: a novel class of bacterial lipids, Acc. Chem. Res. 25, 403–408.
- Pascal, S., Taton, M., Rahier, A. (1993) Plant sterol biosynthesis. Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation, J. Biol. Chem. 268, 1639–1654.
- Patel, N. J., Britton, G., Goodwin, T. W. (1983) Use of deuterium labelling from deuterium oxide to demonstrate carotenoid transformation in photosynthetic bacteria, Biochim. Biophys. Acta 760, 92–96.
- Pedersen, J. I., Gustafsson, J. (1980) Conversion of 3α,7α,12α-trihydroxy-5β-cholestanoic acid into cholic acid by rat liver peroxisomes, FEBS Lett. 121, 345–348.
- Penning, T. M., Abrams, W. R., Pawlowski, J. E. (1991) Affinity labeling of 3α-hydroxysteroid dehydrogenase with 3α-bromoacetoxyandrosterone and 11α-bromoacetoxyprogesterone. Isolation and sequence of active site peptides containing reactive cysteines; sequence confirmation using nucleotide sequence from a cDNA clone, J. Biol. Chem. 266, 8826–8834.
- Pinto, W. J., Nes, W. R. (1983) Stereochemical specificity for sterols in Saccharomyces cerevisiae, J. Biol.Chem. 258, 4472–4476.
- Pinto, W. J., Lozano, R., Sekula, B. C., Nes, W. R. (1983) Stereochemically distinct roles for sterol in Saccharomyces cerevisiae, Biochem. Biophys. Res. Commun. 112, 47–54.
- Poon, W. W., Barkovich, R. J., Hsu, A. Y., Frankel, A., Lee, P. T. et al. (1999) Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis, J. Biol. Chem. 274, 21665–21672.
-
Poralla, K.
(1999)
, Cycloartenol and other triterpene cyclases, in: Comprehensive Natural Products Chemistry, Vol. 2 ( S.D. Barton, K. Nakanishi, O. Meth-Cohn, Eds.), pp. 299–319. Oxford: Elsevier.
10.1016/B978-0-08-091283-7.00046-1 Google Scholar
- Poulter, C. D., Hughes, J. M. (1977) Model studies of the biosynthesis of non-head-to-tail terpenes. Stereochemistry of the head-to-head rearrangement, J. Am. Chem. Soc. 99, 3830–3837.
- Prydz, K., Kase, B. F., Bjorkhem, I., Pedersen, J. I. (1988) Subcellular localization of 3α,7α-dihydroxy- and 3α,7α,12α-trihydroxy-5β-cholestanoyl-coenzyme A ligase(s) in rat liver, J. Lipid Res. 29, 997–1004.
- Pullarkat, R. K., Reha, H., Pullarkat, P. S. (1984) Age-associated increase of free dolichol levels in mice, Biochim. Biophys. Acta 793, 494–496.
- Qureshi, A. A., Beytia, E., Porter, J. W. (1973) Squalene synthetase. II. Purification and properties of baker's yeast enzyme, J. Biol. Chem. 248, 1848–1855.
- Rahier, A., Genot, J. C., Schuber, F., Benveniste, P., Narula, A. S. (1984) Inhibition of S-adenosyl-l-methionine sterol-C-24-methyltransferase by analogues of a carbocationic ion high-energy intermediate. Structure activity relationships for C-25 heteroatoms (N, As, S) substituted triterpenoid derivatives, J. Biol. Chem. 259, 15215–15223.
- Rahier, A., Taton, M., Bouvier-Nave, P., Schmitt, P., Benveniste, P. et al. (1986) Design of high energy intermediate analogues to study sterol biosynthesis in higher plants, Lipids 21, 52–62.
- Reddy, V. V., Caspi, R. (1976) The mechanism of C-5(6) double bond introduction in the biosynthesis of cholesterol by rat liver microsomes, Eur. J. Biochem. 69, 577582.
- Robinson, G. W., Tsay, Y. H., Kienzle, B. K., Smith-Monroy, C. A., Bishop, R. W. (1993) Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation, Mol. Cell Biol. 13, 2706–2717.
- Rohmer, M., Bisseret, P., Sutter, B. (1991) The hopanoids, bacterial triterpenoids, and the biosynthesis of isoprenic units in prokaryotes, Prog. Drug Res. 37, 271–285.
- Rohmer, M., Knani, M., Simonin, P., Sutter, B., Sahm, H. (1993) Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate, Biochem. J. 295, 517–524.
- Rohmer, M., Seemann, M., Horbach, S., Bringer-Mayer, S., Sahm, H. (1996) Glyceraldehyde-3-phosphate and pyruvate as precursors of terpenoid biosynthesis, J. Am. Chem. Soc. 118, 2564–2566.
- Rupar, C. A., Carroll, K. K. (1978) Occurrence of dolichol in human tissues, Lipids 13, 291–293.
- Russell, D. W. (1992) Cholesterol biosynthesis and metabolism, Cardiovascular drugs and Theraph. 6, 103–110.
- Russell, D. W., Setchell, K. D. (1992) Bile acid biosynthesis, Biochemistry 31, 4737–4749.
- Ruzicka, J. (1953) The isoprene rule and the biosynthesis of terpenic compounds, Experientia 9, 357–367.
- Sacchettini, J. C., Poulter, C. D. (1997) Creating isoprenoid diversity, Science 277, 1788–1789.
- Sagami, H., Lennarz, W. J. (1987) Glycoprotein synthesis in Drosophila Kc cells. Biosynthesis of dolichol-linked saccharides, J. Biol. Chem. 262, 15610–15607.
- Sagami, H., Kurisaki, A., Ogura, K. (1993) Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver, J. Biol. Chem. 268, 10109–10113.
- Sandmann, G. (1994) Carotenoid biosynthesis in microoganisms and plants, Eur. J. Biochem. 233, 7–24.
- Sasiak, K., Rilling, H. C. (1988) Purification to homogeneity and some properties of squalene synthetase, Arch. Biochem. Biophys. 260, 622–627.
-
Sato, M.,
Sato, K.,
Nishikawa, S.,
Hirata, A.,
Kato, J.,
Nakano, A.
(1999)
The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis,
Mol. Cell Biol. 19,
71–83.
10.1128/MCB.19.1.471 Google Scholar
- Scallen, T. J., Dean, W. J., Shuster, M. W. (1968) Enzymatic conversion of squalene to cholesterol by an acetone powder of rat liver microsomes, J. Biol. Chem. 243, 5202–5206.
- Schmidhauser, T. J., Lauter, F. R., Schumacher, M., Zhou, W., Russo, V. E., Yanofsky, C. (1994) Characterization of al-2, the phytoene synthase gene of Neurospora crassa. Cloning, sequence analysis, and photoregulation, J. Biol. Chem. 269, 12060–12066.
- Schoenheimer, R., Breusch, F. (1933) Synthesis and destruction of cholesterol in the organism, J. Biol. Chem. 103, 439–448.
- Schram, A. W., Goldfischer, S., Van Roermund, C. W. T., Brounwer-Kelder, E. M., Collins, J. et al. (1987) Human peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency, Proc. Natl. Acad. Sci. USA 84, 2494–2496.
- Schwender, J., Seemann, M., Lichtenthaler, H. K., Rohmer, M. (1996) Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/glyceraldehyde-3-phosphate non-mevalonate pathway in the green alga Scenedesmus obliquus, Biochem. J. 316, 73–80.
- Scolnik, P. A., Walker, M. A., Marrs, B. L. (1980) Biosynthesis of carotenoids derived from neurosporene in Rhodopseudomonas capsulata, J. Biol. Chem. 255, 2427–2432.
- Shechter, I., Bloch, K. (1971) Solubilization and purification of trans-farnesyl pyrophosphate-squalene synthetase, J. Biol. Chem. 246, 7690–7696.
- Shimizu, N., Koyama, T., Ogura, K. (1998) Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases, J. Biol. Chem. 273, 19476–19481.
- Shineberg, B., Yoiung, I. G. (1976) Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli, Biochemistry 15, 2754–2758.
- Shneour, E. A., Zabin, I. (1959) The biosynthesis of lycopene in tomato homogenates, J. Biol. Chem. 234, 770–773.
- Siiteri, P. K., Thompson, E. A. (1975) Studies of human placental aromatase, J. Steroid Biochem. 6, 317–322.
- Simpson, E. R. (1979) Cholesterol side-chain cleavage, cytochrome P450, and the control of steroidogenesis, Mol. Cell Endocrinol. 13, 213–227.
- Soltis, D. A., McMahon, G., Caplan, S. L., Dudas, D. A., Chamberlin, H. A. et al. (1995) Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems, Arch. Biochem. Biophys. 316, 713–723.
- Spurgeon, S. L., Porter, J. W. (1983) Biosynthesis of carotenoids, in: Biosynthesis of Isoprenoid Compounds, Vol. 2 ( J. W. Porter, S. L. Spurgeon, Eds.), pp. 1–122. New York: John Wiley & Sons.
- Stoll, J., Rosenwald, A. G., Krag, S. S. (1988) A Chinese hamster ovary cell mutant F2A8 utilizes polyprenol rather than dolichol for its lipid-dependent asparagine-linked glycosylation reactions, J. Biol. Chem. 263, 10774–10782.
- Straub, O. (1987) List of carotenoids, in: Key to Carotenoids ( H. Pfander, Ed.), 2nd Edn., pp. 11–296. Basel, Switzerland: Birkhäuser Verlag.
- Suzuki, K., Okada, K., Kamiya, Y., Zhu, X. F., Nakagawa, T.et al. (1997) Analysis of the decaprenyl diphosphate synthase (dps) gene in fission yeast suggests a role of ubiquinone as an antioxidant, J. Biochem. (Tokyo) 121, 496–505.
- Swiezewska, E., Sasak, W., Mankowski, T., Jankowski, W., Vogtman, T. et al. (1994) The search for plant polyprenols, Acta Biochim. Pol. 41, 221–260.
- Takahashi, I., Ogura, K. (1982) Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase, J. Biochem. (Tokyo) 92, 1527–1537.
- Taniguchi, S., Hoshita, N., Okuda, K. (1973) Enzymatic characteristics of CO-sensitive 26-hydroxylase system for 5β-cholestane-3α,7α,12α-triol in rat-liver mitochondria and its intramitochondrial localization, Eur. J. Biochem. 40, 607–617.
- Tarshis, L. C., Yan, M., Poulter, C. D., Saxxhettini, J. C. (1994) Crystal structure of recombinant farnesyl diphosphate synthase at 2.6 Å resolution, Biochemistry 33, 10871–10877.
- Taton, M., Rahier, A. (1991) Properties and structural requirements for substrate specificity of cytochrome P-450-dependent obtusifoliol 14α-demethylase from maize (Zea mays) seedlings, Biochem. J. 277, 483–492.
- Taylor, R. F. (1984) Bacterial triterpenoids, Microbiol. Rev. 48, 181–198.
- Teas, H. J., Bandurski, R. S. (1956) The enzymatic synthesis of rubber, J. Am. Chem. Soc. 78, 3549–3550.
- Thigpen, A. E., Davis, D. L., Milatovich, A., Mendonca, B. B., Imperato-McGinley, J. et al. (1992) Molecular genetics of steroid 5α-reductase 2 deficiency, J. Clin. Invest. 90, 799–809.
- Thompson, J. F., Danley, D. E., Mazzalupo, S., Milos, P. M., Lira, M. E., Harwood, H. J., Jr. (1998) Truncation of human squalene synthase yields active, crystallizable protein, Arch. Biochem. Biophys. 350, 283–290.
- Torssell, K. B. G. (1983) The mevalonic acid pathway. The terpenes, in: Natural Product Chemistry – A Mechanistic and Biosynthetic Approach to Secondary Metabolism ( K. B. G. Torssell, Ed.), pp. 167–225. New York: John Wiley & Sons.
- Trzaskos, J., Kawata, S., Gaylor, J. L. (1986) Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14α-methyl demethylase cytochrome P-450 from hepatic microsomes, J. Biol. Chem. 261, 14651–14657.
-
Wallach, O.
(1887)
Zur Kenntnis der Terpene und der ätherischen Öle,
Justus Liebigs Ann. Chem. 239,
1–54.
10.1002/jlac.18872390102 Google Scholar
- Wedgwood, J. F., Strominger, J. L. (1980) Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichyl pyrophosphate and dolichyl phosphate, J. Biol. Chem. 255, 1120–1123.
- Welsche, A., Leistner, E. (1985) Cell-free synthesis of O-succinylbenzoic acid from iso-chorismic acid, the key reaction in vitamin K2 (menaquinone) biosynthesis, Tetrahedron Lett. 26, 1487–1490.
- White, D. C. (1965) The function of 2-demethyl vitamin K2 in the electron transport system of Haemophilus parainfluenzae, J. Biol. Chem. 240, 1387–1394.
- Wieland, H. (1929) The chemistry of bile acids, Z. Angew. Chem. 42, 421–424.
- Wikvall, K. (1981) Purification and properties of a 3 β-hydroxy-Δ5-C27-steroid oxidoreductase from rabbit liver microsomes, J. Biol. Chem. 256, 3376–3380.
- Wikvall, K. (1984) Hydroxylations in biosynthesis of bile acids. Isolation of a cytochrome P-450 from rabbit liver mitochondria catalyzing 26-hydroxylation of C27-steroids, J. Biol. Chem. 259, 3800–3804.
- Wilton, D. C., Munday, K. A., Skinner, S. H., Akhtar, M. (1968) The biological conversion of 7-dehydrocholesterol into cholesterol and comments on the reduction of double bonds, Biochem. J. 106, 803–810.
- Windaus, A. (1935) Sterol as a starting material for hormones, vitamins, and other physiologically important compounds, Nachr. Ges. Wiss. Göttingen Math.-Physik Klasse III 1, 59–83.
- Wojciechowski, Z. A., Goad, L. J., Goodwin, T. W. (1973) S-adenosyl-l-methionine-cycloartenol methyltransferase activity in cell-free systems from Trebouxia sp. and Scenedesmus obliquus, Biochem. J. 136, 405–412.
- Wolf, D. E., Hoffman, C. H., Aldrich, P. E., Skeggs, H. R., Wright, L. D., Folkers, K. (1957) Determination of structure of β,δ-dihydroxy-β-methylvaleric acid, J. Am. Chem. Soc. 79, 1486–1487.
- Wu, G., Williams, H. D., Zamanian, M., Gibson, F., Poole, R. K. (1992) Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG. Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases, J. Gen. Microbiol. 138, 2101–2112.
- Yamaga, N., Gaylor, J. L. (1978) Characterization of the microsomal steroid-8-ene isomerase of cholesterol biosynthesis, J. Lipid Res. 19, 375–382.
- Yamamoto, S., Bloch, K. (1970) Studies on squalene epoxidase of rat liver, J. Biol. Chem. 245, 1670–1674.
- Yanaihara, T., Troen, P. (1972) Studies of the human testis. I. Biosynthetic pathways for androgen formation in human testicular tissue in vitro, J. Clin. Endocrinol. Metab. 34, 783–792.
- Yoshida, Y., Aoyama, Y. (1984) Yeast cytochrome P-450 catalyzing lanosterol 14α-demethylation. I. Purification and spectral properties, J. Biol. Chem. 259, 1655–1660.
- Zhang, Y. W., Koyama, T., Ogura, K. (1997) Two cistrons of the gerC operon of Bacillus subtilis encode the two subunits of heptaprenyl diphosphate synthase, J. Bacteriol. 179, 1417–1419.
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