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Volumn 63, Issue 11, 1999, Pages 2038-2041

New Cyclization Mechanism for Squalene: A Ring-expansion Step for the Five-membered C-ring Intermediate in Hopene Biosynthesis

Author keywords

2,3 oxidosqualene; Hopene; Squalene; Triterpene cyclase

Indexed keywords

DIPLOPTENE; MUTASE; RECOMBINANT PROTEIN; SQUALENE; SQUALENE HOPENE CYCLASE; SQUALENE-HOPENE CYCLASE; TRITERPENE;

EID: 0033218286     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.2038     Document Type: Article
Times cited : (47)

References (17)
  • 1
    • 12044254693 scopus 로고
    • Enzymatic cycliza-tion of squalene and oxidosqualene to sterols and triterpenes
    • Abe, I., Rohmer, M., and Prestwich, G. D., Enzymatic cycliza-tion of squalene and oxidosqualene to sterols and triterpenes. Chem. Rev., 93, 2189-2206 (1993).
    • (1993) Chem. Rev. , vol.93 , pp. 2189-2206
    • Abe, I.1    Rohmer, M.2    Prestwich, G.D.3
  • 2
    • 0032568049 scopus 로고    scopus 로고
    • Synthesis and enzymatic cyclization of (35)11 -fluoro-2,3-oxidosqualene
    • Robustell, B., Abe, I., and Prestwich, G. D., Synthesis and enzymatic cyclization of (35)11 -fluoro-2,3-oxidosqualene. Tetrahedron Lett., 39, 957-960 (1998).
    • (1998) Tetrahedron Lett. , vol.39 , pp. 957-960
    • Robustell, B.1    Abe, I.2    Prestwich, G.D.3
  • 3
    • 0033591019 scopus 로고    scopus 로고
    • The cyclization mechanism of squalene in hopene biosynthesis: The terminal methyl groups are critical to the correct folding of this substrate both for the formation of the five-membered E-ring and for the initiation of the poly-cyclization reaction
    • Hoshino, T. and Kondo, T., The cyclization mechanism of squalene in hopene biosynthesis: the terminal methyl groups are critical to the correct folding of this substrate both for the formation of the five-membered E-ring and for the initiation of the poly-cyclization reaction. J. Chem. Soc. Chem. Commun., 731-732 (1999).
    • (1999) J. Chem. Soc. Chem. Commun. , pp. 731-732
    • Hoshino, T.1    Kondo, T.2
  • 4
    • 0032494971 scopus 로고    scopus 로고
    • On the cyclization mechanism of squalene: A ring expansion process of the five-membered D-ring intermediate
    • Sato, T., Abe, T., and Hoshino, T., On the cyclization mechanism of squalene: a ring expansion process of the five-membered D-ring intermediate. J. Chem. Soc. Chem. Commun., 2617-2618 (1998).
    • (1998) J. Chem. Soc. Chem. Commun. , pp. 2617-2618
    • Sato, T.1    Abe, T.2    Hoshino, T.3
  • 5
    • 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., and Poralla, K., Occurrence of cationic intermediates and deficient control during the enzymatic cyclization of squalene to hopanoids. Angew. Chem. Int. Ed. Engl., 37, 2237-2240 (1998).
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , pp. 2237-2240
    • Pale-Grosdemange, C.1    Feil, C.2    Rohmer, M.3    Poralla, K.4
  • 6
    • 0029962996 scopus 로고    scopus 로고
    • Conversion of a C-20 2,3-ox-idosqualene 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. and Cheng, H., Conversion of a C-20 2,3-ox-idosqualene 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).
    • (1996) Tetrahedron Lett. , vol.37 , pp. 2709-2712
    • Corey, E.J.1    Cheng, H.2
  • 7
    • 21844478741 scopus 로고    scopus 로고
    • Further evidence that the polycycliza-tion reaction by oxidosqualene-lanosterol cyclase proceeds via a ring expansion of the 5-membered C-ring formed by Markov-nikov closure. On the enzymic products of the oxidosqualene analogue having an ethyl residue at the 15-position
    • Hoshino, T. and Sakai, Y., Further evidence that the polycycliza-tion reaction by oxidosqualene-lanosterol cyclase proceeds via a ring expansion of the 5-membered C-ring formed by Markov-nikov closure. On the enzymic products of the oxidosqualene analogue having an ethyl residue at the 15-position. J. Chem. Soc. Chem. Commun., 1591-1592 (1998).
    • (1998) J. Chem. Soc. Chem. Commun. , pp. 1591-1592
    • Hoshino, T.1    Sakai, Y.2
  • 8
    • 0030769202 scopus 로고    scopus 로고
    • Structure and function of a squalene cyclase
    • Wendt, K. U., Poralla, K., and Schulz, G. E., Structure and function of a squalene cyclase. Science, 277, 1811-1815 (1997).
    • (1997) Science , vol.277 , pp. 1811-1815
    • Wendt, K.U.1    Poralla, K.2    Schulz, G.E.3
  • 9
    • 0033548169 scopus 로고    scopus 로고
    • The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution
    • Wendt, K. U., Lenhart, A., and Schulz, G. E., The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution. J. Mol Biol, 286, 175-187 (1999).
    • (1999) J. Mol Biol , vol.286 , pp. 175-187
    • Wendt, K.U.1    Lenhart, A.2    Schulz, G.E.3
  • 10
    • 0031992366 scopus 로고    scopus 로고
    • Overexpression of squalene-hopene cyclase by the pET vector in Escherichia coli and first identification of tryptophan and aspartic acid residues in the QW motif as active sites
    • Sato, T., Kanai, Y., and Hoshino, T., Overexpression of squalene-hopene cyclase by the pET vector in Escherichia coli and first identification of tryptophan and aspartic acid residues in the QW motif as active sites. Biosci. Biotechnol Biochem., 62, 407-411 (1998).
    • (1998) Biosci. Biotechnol Biochem. , vol.62 , pp. 407-411
    • Sato, T.1    Kanai, Y.2    Hoshino, T.3
  • 11
    • 0033161350 scopus 로고    scopus 로고
    • Kinetic studies on the function of all the conserved tryptophans involved inside and outside the QW motifs of squalene-hopene cyclase: Stabilizing effect of the protein structure against thermal denaturation
    • Sato, T. and Hoshino, T., Kinetic studies on the function of all the conserved tryptophans involved inside and outside the QW motifs of squalene-hopene cyclase: stabilizing effect of the protein structure against thermal denaturation. Biosci. Biotechnol Biochem., 63, 1171-1180 (1999).
    • (1999) Biosci. Biotechnol Biochem. , vol.63 , pp. 1171-1180
    • Sato, T.1    Hoshino, T.2
  • 12
    • 0029854776 scopus 로고    scopus 로고
    • Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase
    • Feil, C., Sussmuth, R., Jung, G., and Poralla, K., Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase. Eur. J. Biochem., 242, 51-55 (1996).
    • (1996) Eur. J. Biochem. , vol.242 , pp. 51-55
    • Feil, C.1    Sussmuth, R.2    Jung, G.3    Poralla, K.4
  • 13
    • 0033548668 scopus 로고    scopus 로고
    • Altered product pattern of a squalene-hopene cyclase by mutagenesis of active site residues
    • Merkofer, T., Pale-Grosdemange, C., Wendt, K. U., Rohmer, M., and Poralla, K., Altered product pattern of a squalene-hopene cyclase by mutagenesis of active site residues. Tetrahedron Lett., 40, 2121-2124 (1999).
    • (1999) Tetrahedron Lett. , vol.40 , pp. 2121-2124
    • Merkofer, T.1    Pale-Grosdemange, C.2    Wendt, K.U.3    Rohmer, M.4    Poralla, K.5
  • 14
    • 85009545987 scopus 로고    scopus 로고
    • The structures of tricyclic products 8 and 9 have not been determined in ref. 13. We have independently reported the function of Phe601, described here, at the annual meeting of Japan Society for Biosci., Biotechnol., and Agrochem. March, 1999, Fukuoka, Japan. Abstract p. 306. The GC pattern of mutant F601A, which was constructed by us, was the same as that in the ref. 13
    • The structures of tricyclic products 8 and 9 have not been determined in ref. 13. We have independently reported the function of Phe601, described here, at the annual meeting of Japan Society for Biosci., Biotechnol., and Agrochem. March, 1999, Fukuoka, Japan. Abstract p. 306. The GC pattern of mutant F601A, which was constructed by us, was the same as that in the ref. 13.
  • 15
    • 85009586046 scopus 로고    scopus 로고
    • c (ppm), C-8 (44.38), C-9 (59.61), C-10 (37.45), C-12 (25.19), C-13 (60.12), C-14 (85.35), C-15 (38.30), C-16 (26.63), C-17 (65.98), C-21 (26.63), C-22 (24.50). No NOE between H-13 and H-9 suggests the endo-orientation for the THF moiety
    • c (ppm), C-8 (44.38), C-9 (59.61), C-10 (37.45), C-12 (25.19), C-13 (60.12), C-14 (85.35), C-15 (38.30), C-16 (26.63), C-17 (65.98), C-21 (26.63), C-22 (24.50). No NOE between H-13 and H-9 suggests the endo-orientation for the THF moiety.
  • 16
    • 0030781006 scopus 로고    scopus 로고
    • Computational investigations of carbenium ion reactions relevant to sterol biosynthesis
    • Jenson, C. and Jorgensen, W. L., Computational investigations of carbenium ion reactions relevant to sterol biosynthesis. J. Am. Chem. Soc., 119, 10846-10854 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10846-10854
    • Jenson, C.1    Jorgensen, W.L.2
  • 17
    • 0030033588 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: Anew view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. A., Cation-π interactions in chemistry and biology: anew view of benzene, Phe, Tyr, and Trp. Science, 271, 163-168 (1996).
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.