메뉴 건너뛰기




Volumn 11, Issue 1, 2004, Pages 121-126

Conversion of Squalene to the Pentacarbocyclic Hopene

Author keywords

[No Author keywords available]

Indexed keywords


EID: 1142281936     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2003.12.013     Document Type: Article
Times cited : (104)

References (33)
  • 1
    • 0002317514 scopus 로고    scopus 로고
    • Natural products (secondary metabolites)
    • B. Buchanan, W. Gruissem, & R. Jones. New York: Wiley & Sons
    • Croteau R., Kutchan T.M., Lewis N.G. Natural products (secondary metabolites). Buchanan B., Gruissem W., Jones R. Biochemistry and Molecular Biology of Plants. 2000;1250-1315 Wiley & Sons, New York.
    • (2000) Biochemistry and Molecular Biology of Plants , pp. 1250-1315
    • Croteau, R.1    Kutchan, T.M.2    Lewis, N.G.3
  • 2
    • 0030769202 scopus 로고    scopus 로고
    • Structure and function of squalene cyclase
    • Wendt K.U., Poralla K., Schulz G.E. Structure and function of squalene cyclase. Science. 277:1997;1811-1815.
    • (1997) Science , vol.277 , pp. 1811-1815
    • Wendt, K.U.1    Poralla, K.2    Schulz, G.E.3
  • 3
    • 0030796451 scopus 로고    scopus 로고
    • Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase
    • Starks C.M., Back K., Chappel J., Noel J.P. Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase. Science. 277:1997;1815-1820.
    • (1997) Science , vol.277 , pp. 1815-1820
    • Starks, C.M.1    Back, K.2    Chappel, J.3    Noel, J.P.4
  • 4
    • 0030777210 scopus 로고    scopus 로고
    • Crystal structure of pentalenene synthase: Mechanistic insights on terpenoid cyclization reactions in biology
    • Lesburg C.A., Zhai G., Cane D.E., Christianson D.W. Crystal structure of pentalenene synthase. mechanistic insights on terpenoid cyclization reactions in biology Science. 277:1997;1820-1824.
    • (1997) Science , vol.277 , pp. 1820-1824
    • Lesburg, C.A.1    Zhai, G.2    Cane, D.E.3    Christianson, D.W.4
  • 5
    • 0034682766 scopus 로고    scopus 로고
    • Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti
    • Caruthers J.M., Kang I., Rynkiewicz M.J., Cane D.E., Christianson D.W. Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti. J. Biol. Chem. 275:2000;25533-25539.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25533-25539
    • Caruthers, J.M.1    Kang, I.2    Rynkiewicz, M.J.3    Cane, D.E.4    Christianson, D.W.5
  • 6
    • 0035923697 scopus 로고    scopus 로고
    • Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade
    • Rynkiewicz M.J., Cane D.E., Christianson D.W. Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade. Proc. Natl. Acad. Sci. USA. 98:2001;13543-13548.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13543-13548
    • Rynkiewicz, M.J.1    Cane, D.E.2    Christianson, D.W.3
  • 8
    • 0001651238 scopus 로고
    • The cyclization of squalene in cholesterol synthesis
    • Woodward R.B., Bloch K. The cyclization of squalene in cholesterol synthesis. J. Am. Chem. Soc. 75:1953;2023-2024.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 2023-2024
    • Woodward, R.B.1    Bloch, K.2
  • 9
    • 12044254693 scopus 로고
    • Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes
    • Abe I., Rohmer M., Prestwich G.D. Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes. Chem. Rev. 90:1993;2189-2206.
    • (1993) Chem. Rev. , vol.90 , pp. 2189-2206
    • Abe, I.1    Rohmer, M.2    Prestwich, G.D.3
  • 11
    • 0033548169 scopus 로고    scopus 로고
    • The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution
    • Wendt K.U., Lenhart A., Schulz G.E. The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol. 286:1999;175-187.
    • (1999) J. Mol. Biol. , vol.286 , pp. 175-187
    • Wendt, K.U.1    Lenhart, A.2    Schulz, G.E.3
  • 13
    • 0029854776 scopus 로고    scopus 로고
    • Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase
    • Feil C., Süssmuth R., Jung G., Poralla K. Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase. Eur. J. Biochem. 242:1996;51-55.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 51-55
    • Feil, C.1    Süssmuth, R.2    Jung, G.3    Poralla, K.4
  • 14
    • 0023216282 scopus 로고
    • Synthesis and biological activity of azasqualenes, bis-azasqualenes and derivatives
    • Ceruti M., Balliano G., Viola F., Cattel L., Gerst N., Schuber F. Synthesis and biological activity of azasqualenes, bis-azasqualenes and derivatives. Eur. J. Med. Chem. 22:1987;199-208.
    • (1987) Eur. J. Med. Chem. , vol.22 , pp. 199-208
    • Ceruti, M.1    Balliano, G.2    Viola, F.3    Cattel, L.4    Gerst, N.5    Schuber, F.6
  • 15
    • 0036015845 scopus 로고    scopus 로고
    • Crystal structure of a squalene cyclase in complex with the potential anticholesteremic drug Ro48-8071
    • Lenhart A., Weihofen W.A., Pleschke A.E.W., Schulz G.E. Crystal structure of a squalene cyclase in complex with the potential anticholesteremic drug Ro48-8071. Chem. Biol. 10:2002;639-645.
    • (2002) Chem. Biol. , vol.10 , pp. 639-645
    • Lenhart, A.1    Weihofen, W.A.2    Pleschke, A.E.W.3    Schulz, G.E.4
  • 16
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley S.K., Petsko G.A. Aromatic-aromatic interaction. A mechanism of protein structure stabilization Science. 229:1985;23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 18
    • 0038025347 scopus 로고    scopus 로고
    • Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase
    • Lenhart A., Reinert D.J., Aebi J.D., Dehmlow H., Morand O.H., Schulz G.E. Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase. J. Med. Chem. 46:2003;2083-2092.
    • (2003) J. Med. Chem. , vol.46 , pp. 2083-2092
    • Lenhart, A.1    Reinert, D.J.2    Aebi, J.D.3    Dehmlow, H.4    Morand, O.H.5    Schulz, G.E.6
  • 19
    • 0030781006 scopus 로고    scopus 로고
    • Computational investigations of carbenium ion reactions relevant to sterol biosynthesis
    • Jenson C., Jorgensen W.L. Computational investigations of carbenium ion reactions relevant to sterol biosynthesis. J. Am. Chem. Soc. 119:1997;10846-10854.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10846-10854
    • Jenson, C.1    Jorgensen, W.L.2
  • 20
    • 0038341792 scopus 로고    scopus 로고
    • Formation of the C ring in the lanosterol biosynthesis from squalene
    • Hess B.A. Jr. Formation of the C ring in the lanosterol biosynthesis from squalene. Org. Lett. 5:2003;165-167.
    • (2003) Org. Lett. , vol.5 , pp. 165-167
    • Hess, B.A.Jr.1
  • 21
    • 0037019526 scopus 로고    scopus 로고
    • Concomitant C-ring expansion and D-ring formation in lanosterol biosynthesis from squalene without violation of Markovnikov's rule
    • Hess B.A. Jr. Concomitant C-ring expansion and D-ring formation in lanosterol biosynthesis from squalene without violation of Markovnikov's rule. J. Am. Chem. Soc. 124:2002;10286-10287.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10286-10287
    • Hess, B.A.Jr.1
  • 22
    • 0031709419 scopus 로고    scopus 로고
    • Occurrence of cationic intermediates and deficient control during the enzymatic cyclization of squalene into hopenoids
    • Pale-Grosdemange C., Feil C., Rohmer M., Poralla K. Occurrence of cationic intermediates and deficient control during the enzymatic cyclization of squalene into hopenoids. Angew. Chem. Int. Ed. Engl. 37:1998;2237-2240.
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , pp. 2237-2240
    • Pale-Grosdemange, C.1    Feil, C.2    Rohmer, M.3    Poralla, K.4
  • 23
    • 0037148784 scopus 로고    scopus 로고
    • Squalene-hopene cyclase: Catalytic mechanism and substrate recognition
    • Camb.
    • Hoshino, T., and Sato, T. (2002). Squalene-hopene cyclase: catalytic mechanism and substrate recognition. Chem. Commun. (Camb.), 291-301.
    • (2002) Chem. Commun. , pp. 291-301
    • Hoshino, T.1    Sato, T.2
  • 25
    • 0030891856 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of squalene-hopene cyclase from Alicyclobacillus acidocaldarius
    • Wendt K.U., Feil C., Lenhart A., Poralla K., Schulz G.E. Crystallization and preliminary X-ray crystallographic analysis of squalene-hopene cyclase from Alicyclobacillus acidocaldarius. Protein Sci. 6:1997;722-724.
    • (1997) Protein Sci. , vol.6 , pp. 722-724
    • Wendt, K.U.1    Feil, C.2    Lenhart, A.3    Poralla, K.4    Schulz, G.E.5
  • 26
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:1993;795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 28
    • 0030158429 scopus 로고    scopus 로고
    • PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules
    • van Aalten D.M.F., Bywater R., Findlay J.B.C., Hendlich M., Hooft R.W.W., Vriend G. PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J. Comput Aided Mol. Des. 10:1996;255-262.
    • (1996) J. Comput Aided Mol. Des. , vol.10 , pp. 255-262
    • Van Aalten, D.M.F.1    Bywater, R.2    Findlay, J.B.C.3    Hendlich, M.4    Hooft, R.W.W.5    Vriend, G.6
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: A program for model and data visualization using persistence of vision ray-tracing
    • Fenn T.D., Ringe D., Petsko G.A. POVScript+. a program for model and data visualization using persistence of vision ray-tracing J. Appl. Crystallogr. 36:2003;944-947.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 32
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster 3D. Photorealistic molecular graphics Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 33
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner M.F., Olson A.J., Spehner J.-C. Reduced surface. An efficient way to compute molecular surfaces Biopolymers. 38:1996;305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.-C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.