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Volumn 6, Issue 6, 1999, Pages 333-341

The binding site for an inhibitor of squalene:hopene cyclase determined using photoaffinity labeling and molecular modeling

Author keywords

Active site mapping; Benzophenone; Enzyme inhibitor; Triterpene biosynthesis

Indexed keywords

BIOSYNTHESIS; ENZYME INHIBITOR; MOLECULAR AND CELLULAR STRUCTURE; PHOTOAFFINITY LABELING; SQUALENE HOPENE CYCLASE;

EID: 0033150533     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80045-3     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 12044254693 scopus 로고
    • Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes
    • Abe, I., Rohmer, M. & Prestwich, G.D. (1993). Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes. Chem. Rev. 93, 2189-2206.
    • (1993) Chem. Rev. , vol.93 , pp. 2189-2206
    • Abe, I.1    Rohmer, M.2    Prestwich, G.D.3
  • 3
    • 0028945656 scopus 로고
    • Chemical structure of sterols that activate oocyte meiosis
    • Byskov, A.G., et al., & Roed, T. (1995). Chemical structure of sterols that activate oocyte meiosis. Nature 374, 559-562.
    • (1995) Nature , vol.374 , pp. 559-562
    • Byskov, A.G.1    Roed, T.2
  • 5
    • 0022447239 scopus 로고
    • Characterization and partial purification of squalene-hopene cyclase from Bacillus acidocaldarius
    • Seckler, B. & Poralla, K. (1986). Characterization and partial purification of squalene-hopene cyclase from Bacillus acidocaldarius. Biophys. Biochim. Acta 881, 356-363.
    • (1986) Biophys. Biochim. Acta , vol.881 , pp. 356-363
    • Seckler, B.1    Poralla, K.2
  • 6
    • 0026576348 scopus 로고
    • Cloning, expression, and sequencing of squalene-hopene cyclase, a key enzyme in triterpenoid metabolism
    • Ochs, D., Kaletta, C., Entian, K.-D., Beck-Sickinger, A. & Poralla, K. (1992). Cloning, expression, and sequencing of squalene-hopene cyclase, a key enzyme in triterpenoid metabolism. J. Bacteriol. 174, 298-302.
    • (1992) J. Bacteriol. , vol.174 , pp. 298-302
    • Ochs, D.1    Kaletta, C.2    Entian, K.-D.3    Beck-Sickinger, A.4    Poralla, K.5
  • 7
    • 0028817559 scopus 로고
    • Zymomonas mobilis squalene-hopene cyclase gene (shc): Cloning, DNA sequence analysis, and expression in Escherichia coli
    • Reipen, I.G., Poralla, K., Sahm, H. & Sprenger, G.A. (1995). Zymomonas mobilis squalene-hopene cyclase gene (shc): Cloning, DNA sequence analysis, and expression in Escherichia coli. Microbiology 141, 155-161.
    • (1995) Microbiology , vol.141 , pp. 155-161
    • Reipen, I.G.1    Poralla, K.2    Sahm, H.3    Sprenger, G.A.4
  • 8
    • 0032579970 scopus 로고    scopus 로고
    • Squalene-hopene cyclase from Methylococcus capsulatus (Bath): A bacterium producing hopanoids and steroids
    • Tippelt, A., Jahnke, L. & Poralla, K. (1998). Squalene-hopene cyclase from Methylococcus capsulatus (Bath): A bacterium producing hopanoids and steroids. Biophys. Biochim. Acta. 1391, 223-232.
    • (1998) Biophys. Biochim. Acta. , vol.1391 , pp. 223-232
    • Tippelt, A.1    Jahnke, L.2    Poralla, K.3
  • 9
    • 1842328052 scopus 로고    scopus 로고
    • Squalene-hopene cyclase from Bradyrhizobium japonicum: Cloning, expression, sequence analysis and comparison to other triterpenoid cyclases
    • Perzl, M., Muller, P., Poralla, K. & Kannenberg, E.L. (1997). Squalene-hopene cyclase from Bradyrhizobium japonicum: Cloning, expression, sequence analysis and comparison to other triterpenoid cyclases. Microbiology 143, 1235-1242.
    • (1997) Microbiology , vol.143 , pp. 1235-1242
    • Perzl, M.1    Muller, P.2    Poralla, K.3    Kannenberg, E.L.4
  • 10
    • 0003693962 scopus 로고    scopus 로고
    • Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids
    • Perzl, M., et al., & Kannenberg, E.L. (1998). Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids. Biochim. Biophys. Acta 1393, 108-118.
    • (1998) Biochim. Biophys. Acta , vol.1393 , pp. 108-118
    • Perzl, M.1    Kannenberg, E.L.2
  • 11
    • 0028280613 scopus 로고
    • The possible role of a repetitive amino acid motif in evolution of triterpenoid cyclases
    • Poralla, K. (1994). The possible role of a repetitive amino acid motif in evolution of triterpenoid cyclases. Bioorg. Med. Chem. Lett. 4, 285-290.
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 285-290
    • Poralla, K.1
  • 13
    • 0000538827 scopus 로고    scopus 로고
    • Squalene epoxidase and oxidosqualene:lanosterol cyclase. Key enzymes in cholesterol biosynthesis
    • Barton, D.H.R. & Nakanishi, K., eds, in press.
    • Abe, I. & Prestwich, G.D. (1999). Squalene epoxidase and oxidosqualene:lanosterol cyclase. Key enzymes in cholesterol biosynthesis. In Comprehensive Natural Products Chemistry; (Barton, D.H.R. & Nakanishi, K., eds), in press.
    • (1999) Comprehensive Natural Products Chemistry
    • Abe, I.1    Prestwich, G.D.2
  • 14
    • 0029854776 scopus 로고    scopus 로고
    • Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase
    • Feil, C., Sussmuth, R., Jung, G. & Poralla, K. (1996). Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase. Eur. J. Biochem. 242, 51-55.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 51-55
    • Feil, C.1    Sussmuth, R.2    Jung, G.3    Poralla, K.4
  • 15
    • 0030984243 scopus 로고    scopus 로고
    • Studies on the substrate binding segments and catalytic action of lanosterol synthase. Affinity labeling with carbocations derived from mechanism-based analogs of 2,3-oxidosqualene and site-directed mutagenesis probes
    • Corey, E.J., Cheng, H.M., Baker, C.H., Matsuda, S.P.T., Li, D. & Song, X.L. (1997). Studies on the substrate binding segments and catalytic action of lanosterol synthase. Affinity labeling with carbocations derived from mechanism-based analogs of 2,3-oxidosqualene and site-directed mutagenesis probes. J. Am. Chem. Soc. 119, 1289-1296.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1289-1296
    • Corey, E.J.1    Cheng, H.M.2    Baker, C.H.3    Matsuda, S.P.T.4    Li, D.5    Song, X.L.6
  • 16
    • 0001214229 scopus 로고
    • Bioorganic characterization and mechanism of the 2,3-oxidosqualene-lanosterol conversion
    • van Tamelen, E.E. (1982). Bioorganic characterization and mechanism of the 2,3-oxidosqualene-lanosterol conversion. J. Am. Chem. Soc. 104, 6480-6481.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6480-6481
    • Van Tamelen, E.E.1
  • 17
    • 0032577014 scopus 로고    scopus 로고
    • Theoretical evidence for a concerted mechanism of the oxirane cleavage and A-ring formation in oxidosqualene cyclization
    • Gao, D.Q., Pan, Y.K., Byun, K. & Gao, J.L. (1998). Theoretical evidence for a concerted mechanism of the oxirane cleavage and A-ring formation in oxidosqualene cyclization. J. Am. Chem. Soc. 120, 4045-4046.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4045-4046
    • Gao, D.Q.1    Pan, Y.K.2    Byun, K.3    Gao, J.L.4
  • 18
    • 0030781006 scopus 로고    scopus 로고
    • Computational investigations of carbenium ion reactions relevant to sterol biosynthesis
    • Jenson, C. & Jorgensen, W.L. (1997). Computational investigations of carbenium ion reactions relevant to sterol biosynthesis. J. Am. Chem. Soc. 119, 10846-10854.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10846-10854
    • Jenson, C.1    Jorgensen, W.L.2
  • 19
    • 0029962996 scopus 로고    scopus 로고
    • Conversion of a C-20 2,3-oxidosqualene analog to tricyclic structures with a five-membered C-ring by lanosterol synthase. Further evidence for a C-ring expansion step in sterol biosynthesis
    • Corey, E.J. & Cheng, H.M. (1996). Conversion of a C-20 2,3-oxidosqualene analog to tricyclic structures with a five-membered C-ring by lanosterol synthase. Further evidence for a C-ring expansion step in sterol biosynthesis. Tetrahedron Lett. 37, 2709-2712.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 2709-2712
    • Corey, E.J.1    Cheng, H.M.2
  • 20
    • 0028841523 scopus 로고
    • New insights regarding the cyclization pathway for sterol biosynthesis from (S)-2,3-oxidosqualene
    • Corey, E.J., et al., & Sarshar, S. (1995). New insights regarding the cyclization pathway for sterol biosynthesis from (S)-2,3-oxidosqualene. J. Am. Chem. Soc. 117, 11819-11820.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11819-11820
    • Corey, E.J.1    Sarshar, S.2
  • 21
    • 21844478741 scopus 로고    scopus 로고
    • Further evidence that the polycyclization reaction by OSLC proceeds via a ring expansion
    • Hoshino, T. & Sakai, Y. (1998). Further evidence that the polycyclization reaction by OSLC proceeds via a ring expansion. J. Chem. Soc. Chem. Commun. 1998, 1591-1592.
    • (1998) J. Chem. Soc. Chem. Commun. , vol.1998 , pp. 1591-1592
    • Hoshino, T.1    Sakai, Y.2
  • 22
    • 0031709419 scopus 로고    scopus 로고
    • Occurrence of cationic intermediates and deficient control during the enzymatic cyclization of squalene to hopanoids
    • Pale-Grosdemange, C., Feil, C., Rohmer, M. & Poralla, K. (1998). Occurrence of cationic intermediates and deficient control during the enzymatic cyclization of squalene to hopanoids. Angew. Chem. Int. Ed. 37, 2237-2240.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 2237-2240
    • Pale-Grosdemange, C.1    Feil, C.2    Rohmer, M.3    Poralla, K.4
  • 23
    • 0027979831 scopus 로고
    • Active site mapping of affinity-labeled rat oxidosqualene cyclase
    • Abe, I. & Prestwich, G.D. (1994). Active site mapping of affinity-labeled rat oxidosqualene cyclase. J. Biol. Chem. 269, 802-804.
    • (1994) J. Biol. Chem. , vol.269 , pp. 802-804
    • Abe, I.1    Prestwich, G.D.2
  • 24
    • 2642619387 scopus 로고    scopus 로고
    • Photoaffinity labeling of oxidosqualene cyclase and squalene cyclase by a benzophenone-containing inhibitor
    • Abe, I., Zheng, Y.F. & Prestwich, G.D. (1998). Photoaffinity labeling of oxidosqualene cyclase and squalene cyclase by a benzophenone-containing inhibitor. Biochemistry 37, 5779-5784.
    • (1998) Biochemistry , vol.37 , pp. 5779-5784
    • Abe, I.1    Zheng, Y.F.2    Prestwich, G.D.3
  • 25
    • 0030615072 scopus 로고    scopus 로고
    • Ro 48-8071, a new 2,-oxidosqualene:lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: Comparison to simvastatin
    • Morand, O.H., et al., & Himber, J. (1997). Ro 48-8071, a new 2,-oxidosqualene:lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: Comparison to simvastatin. J. Lipid Res. 38, 373-390.
    • (1997) J. Lipid Res. , vol.38 , pp. 373-390
    • Morand, O.H.1    Himber, J.2
  • 26
    • 0030769202 scopus 로고    scopus 로고
    • Structure and function of a squalene cyclase
    • Wendt, K.U., Poralla, K. & Schulz, G.E. (1997). Structure and function of a squalene cyclase. Science 277, 1811-1815.
    • (1997) Science , vol.277 , pp. 1811-1815
    • Wendt, K.U.1    Poralla, K.2    Schulz, G.E.3
  • 27
    • 0032574793 scopus 로고    scopus 로고
    • Site-directed mutagenesis combined with chemical modification as a strategy for altering the specificity of the S1 and S1′ pockets of subtilisin Bacillus lentus
    • DeSantis, G., Berglund, P., Stabile, M.R., Gold, M. & Jones, J.B. (1998). Site-directed mutagenesis combined with chemical modification as a strategy for altering the specificity of the S1 and S1′ pockets of subtilisin Bacillus lentus. Biochemistry 37, 5968-73.
    • (1998) Biochemistry , vol.37 , pp. 5968-5973
    • DeSantis, G.1    Berglund, P.2    Stabile, M.R.3    Gold, M.4    Jones, J.B.5
  • 28
    • 0032170496 scopus 로고    scopus 로고
    • Stereochemistry of the chloroperoxidase active site: Crystallographic and molecular-modeling studies
    • Sundaramoorthy, M., Terner, J. & Poulos, T.L. (1998). Stereochemistry of the chloroperoxidase active site: Crystallographic and molecular-modeling studies. Chem. Biol. 5, 461-473.
    • (1998) Chem. Biol. , vol.5 , pp. 461-473
    • Sundaramoorthy, M.1    Terner, J.2    Poulos, T.L.3
  • 29
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
    • Dauber-Osguthorpe, P., Roberts, V.A., Osguthorpe, D.J., Wolff, J., Genest, M. & Hagler, A.T. (1988). Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins 4, 31-47.
    • (1988) Proteins , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 30
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly, M. (1993). The molecular surface package. J. Mol. Graph. 11, 139-141.
    • (1993) J. Mol. Graph. , vol.11 , pp. 139-141
    • Connolly, M.1
  • 31
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dormán, G. & Prestwich, G.D. (1994). Benzophenone photophores in biochemistry. Biochemistry 33, 5661-5673.
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dormán, G.1    Prestwich, G.D.2
  • 32
    • 0000632499 scopus 로고
    • Overall mechanism of terpenoid terminal epoxide polycyclizations
    • van Tamelen, E.E. & James, D.R. (1977). Overall mechanism of terpenoid terminal epoxide polycyclizations. J. Am. Chem. Soc. 99, 950-952.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 950-952
    • Van Tamelen, E.E.1    James, D.R.2
  • 33
    • 0031793802 scopus 로고    scopus 로고
    • Mechanism-based inhibitors and other active-site targeted inhibitors of oxidosqualene cyclase and squalene cyclase
    • Abe, I., Zheng, Y.F. & Prestwich, G.D. (1998). Mechanism-based inhibitors and other active-site targeted inhibitors of oxidosqualene cyclase and squalene cyclase. J. Enzym. Inhib. 13, 385-398.
    • (1998) J. Enzym. Inhib. , vol.13 , pp. 385-398
    • Abe, I.1    Zheng, Y.F.2    Prestwich, G.D.3
  • 35
    • 0032520232 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: Manifold chemistry catalyzed by similar enzymes
    • Wendt, K.U. & Schulz, G.E. (1998). Isoprenoid biosynthesis: Manifold chemistry catalyzed by similar enzymes. Structure 6, 127-133.
    • (1998) Structure , vol.6 , pp. 127-133
    • Wendt, K.U.1    Schulz, G.E.2
  • 36
    • 0032414228 scopus 로고    scopus 로고
    • Managing and manipulating carbocations in biology: Terpenoid cyclase structure and mechanism
    • Lesburg, C., Caruther, J., Paschall, C. & Christianson, D. (1998). Managing and manipulating carbocations in biology: Terpenoid cyclase structure and mechanism. Curr. Opin. Struct. Biol. 8, 695-703.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 695-703
    • Lesburg, C.1    Caruther, J.2    Paschall, C.3    Christianson, D.4
  • 37
    • 0030043489 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D.A. (1996). Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp. Science 271, 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 38
    • 0025055546 scopus 로고
    • Inhibitors of 2,3-oxidosqualene lanosterol cyclase as potential antifungal agents
    • Jolidon, S., Polak, A.-M., Guerry, P. & Hartman, P.G. (1989). Inhibitors of 2,3-oxidosqualene lanosterol cyclase as potential antifungal agents. Biochem. Soc. Trans. 18, 47-48.
    • (1989) Biochem. Soc. Trans. , vol.18 , pp. 47-48
    • Jolidon, S.1    Polak, A.-M.2    Guerry, P.3    Hartman, P.G.4
  • 39
    • 0030064188 scopus 로고    scopus 로고
    • Effects of a novel 2,3-oxidosqualene cyclase inhibitor on the regulation of cholesterol biosynthesis in HepG2 cells
    • Mark, M., Muller, P., Maier, R. & Eisele, B. (1996). Effects of a novel 2,3-oxidosqualene cyclase inhibitor on the regulation of cholesterol biosynthesis in HepG2 cells. J. Lipid Res. 37, 148-158.
    • (1996) J. Lipid Res. , vol.37 , pp. 148-158
    • Mark, M.1    Muller, P.2    Maier, R.3    Eisele, B.4
  • 40
    • 0030951557 scopus 로고    scopus 로고
    • Effects of a novel 2,3-oxidosqualene cyclase inhibitor on cholesterol biosynthesis and lipid metabolism in vivo
    • Eisele, B., Budzinski, R., Muller, P., Maier, R. & Mark, M. (1997). Effects of a novel 2,3-oxidosqualene cyclase inhibitor on cholesterol biosynthesis and lipid metabolism in vivo. J. Lipid Res. 38, 564-575.
    • (1997) J. Lipid Res. , vol.38 , pp. 564-575
    • Eisele, B.1    Budzinski, R.2    Muller, P.3    Maier, R.4    Mark, M.5
  • 41
    • 85030367082 scopus 로고    scopus 로고
    • Cyclization mechanism of squalene: A ring expansion process of D-ring formed by Markovnikov closure, proved by site-directed mutagenesis and by using squalene analogue C-27 with hydroxyl group
    • Gifu, Japan.
    • Hoshino, T., Sato, T. & Abe, T. (1998). Cyclization mechanism of squalene: A ring expansion process of D-ring formed by Markovnikov closure, proved by site-directed mutagenesis and by using squalene analogue C-27 with hydroxyl group. 42nd Symposium on the Chemistry of Terpenes, Essential Oils, and Aromatics. pp 266-268. Gifu, Japan.
    • (1998) 42nd Symposium on the Chemistry of Terpenes, Essential Oils, and Aromatics , pp. 266-268
    • Hoshino, T.1    Sato, T.2    Abe, T.3
  • 42
    • 0030710635 scopus 로고    scopus 로고
    • Cyclization of (3S)-29-methylidene-2,3-oxidosqualene by bacterial squalene:hopene cyclase: Irreversible enzyme inactivation and isolation of an unnatural dammarenoid
    • Abe, I., et al, & Prestwich, G.D. (1997). Cyclization of (3S)-29-methylidene-2,3-oxidosqualene by bacterial squalene:hopene cyclase: Irreversible enzyme inactivation and isolation of an unnatural dammarenoid. J. Am. Chem. Soc. 119, 11333-11334.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11333-11334
    • Abe, I.1    Prestwich, G.D.2
  • 43
    • 0025989958 scopus 로고
    • Fifty years of research: A tribute to my co-workers
    • Johnson, W.S. (1991). Fifty years of research: A tribute to my co-workers. Tetrahedron 47, xi-1.
    • (1991) Tetrahedron , vol.47
    • Johnson, W.S.1
  • 44
    • 0033548169 scopus 로고    scopus 로고
    • The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution
    • Wendt, K., Lenhart, A. & Schulz, G. (1999). The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol. 286, 175-187.
    • (1999) J. Mol. Biol. , vol.286 , pp. 175-187
    • Wendt, K.1    Lenhart, A.2    Schulz, G.3


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