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Volumn 63, Issue 12, 1999, Pages 2189-2198

Functional analysis of the DXDDTA motif in squalene-hopene cyclase by site-directed mutagenesis experiments: Initiation site of the polycyclization reaction and stabilization site of the carbocation intermediate of the initially cyclized A-ring

Author keywords

Alicyclobacillus acidocaldarius; DXDDTA motif; Hopene; Oxidosqualene; Squalene

Indexed keywords

MUTASE; SQUALENE HOPENE CYCLASE; SQUALENE-HOPENE CYCLASE;

EID: 0033252974     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.2189     Document Type: Article
Times cited : (67)

References (45)
  • 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
    • 0026576348 scopus 로고
    • Cloning, expression, and sequencing of squalene-ho-pene cyclase, a key enzyme in triterpenoid metabolism
    • Ochs, D., Kaletta, C., Entian, K-D., Beck-Sickinger, A., and Poralla, K., Cloning, expression, and sequencing of squalene-ho-pene cyclase, a key enzyme in triterpenoid metabolism. J. Bac-teriol., 174, 298-302 (1992).
    • (1992) J. Bac-Teriol. , vol.174 , pp. 298-302
    • Ochs, D.1    Kaletta, C.2    Entian, K.-D.3    Beck-Sickinger, A.4    Poralla, K.5
  • 3
    • 0028817559 scopus 로고
    • Zymomonas mobilis squalene-hopene cyclase gene (She): Cloning, DNA sequence analysis, and expression in
    • Reipen, I. G., Poralla, K., Sahm, H., and Sprenger, G. A., Zymomonas mobilis squalene-hopene cyclase gene (she): cloning, DNA sequence analysis, and expression in Escherichia coli. Microbiology, 141, 155-161 (1995).
    • (1995) Escherichia Coli. Microbiology , vol.141 , pp. 155-161
    • Reipen, I.G.1    Poralla, K.2    Sahm, H.3    Sprenger, G.A.4
  • 4
    • 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., and Kannenberg, E. L., Squalene-hopene cyclase from Bradyrhizobium japonicum: cloning, expression, sequence analysis and comparison to other triterpenoid cyclases. Microbiology, 143, 1235-1242 (1997).
    • (1997) Microbiology , vol.143 , pp. 1235-1242
    • Perzl, M.1    Muller, P.2    Poralla, K.3    Kannenberg, E.L.4
  • 5
    • 0032579970 scopus 로고    scopus 로고
    • Squalene-hopene cyclase from Methylococcus capsulatus (Bath): A bacterium producing hopanoids and steroids
    • Tippelt, A., Jahnke, L., and Poralla, K., Squalene-hopene cyclase from Methylococcus capsulatus (Bath): a bacterium producing hopanoids and steroids. Biochem. Biophys. Acta, 1391, 223-232 (1998).
    • (1998) Biochem. Biophys. Acta , vol.1391 , pp. 223-232
    • Tippelt, A.1    Jahnke, L.2    Poralla, K.3
  • 6
    • 84889512873 scopus 로고
    • Nucleotide and deduced amino acid sequences of the oxidosqualene cyclase from Candida albicans
    • Buntel, C. J., and Griffin, J. H., Nucleotide and deduced amino acid sequences of the oxidosqualene cyclase from Candida albicans. J. Am. Chem. Soc., 114, 9711-9713 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9711-9713
    • Buntel, C.J.1    Griffin, J.H.2
  • 8
    • 0028325230 scopus 로고
    • Molecular cloning, characterization, and overexpression of ERG7, the Sac-char omyces cerevisiae gene encoding lanosterol synthase
    • Corey, E. J., Matsuda, S. P. T., and Bartel, B., Molecular cloning, characterization, and overexpression of ERG7, the Sac-char omyces cerevisiae gene encoding lanosterol synthase. Proc. Natl. Acad. Sci. USA, 91, 2211-2215 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2211-2215
    • Corey, E.J.1    Matsuda, S.P.T.2    Bartel, B.3
  • 9
    • 0028283156 scopus 로고
    • Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae
    • Shi, Z., Buntel, C. J., and Griffin, J. H., Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA, 91, 7370-7374 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7370-7374
    • Shi, Z.1    Buntel, C.J.2    Griffin, J.H.3
  • 10
    • 0028888641 scopus 로고
    • Molecular cloning of cDNA encoding rat 2,3-oxido-squalene:Lanosterol cyclase
    • Kusano, M., Shibuya, M., Sankawa, U., and Ebizuka, Y., Molecular cloning of cDNA encoding rat 2,3-oxido-squalene:lanosterol cyclase. Biol. Pharm. Bull., 18, 195-197 (1995).
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 195-197
    • Kusano, M.1    Shibuya, M.2    Sankawa, U.3    Ebizuka, Y.4
  • 11
    • 0029049232 scopus 로고
    • Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA
    • Abe, I., and Prestwich, G. D., Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA. Proc. Natl. Acad. Sci. USA, 92, 9274-9278 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9274-9278
    • Abe, I.1    Prestwich, G.D.2
  • 12
    • 0028842522 scopus 로고
    • Molecular cloning of cDNA encoding human lanosterol synthase
    • Sung, C.K., Shibuya, M., Sankawa, U., and Ebizuka, Y., Molecular cloning of cDNA encoding human lanosterol synthase. Biol. Pharm. Bull., 18, 1459-1461 (1995).
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1459-1461
    • Sung, C.K.1    Shibuya, M.2    Sankawa, U.3    Ebizuka, Y.4
  • 13
    • 0029100941 scopus 로고
    • Molecular cloning of the human gene encoding lanosterol synthase from a liver cDNA library
    • Baker, C. H., Matsuda, S. P. T., Liu, D. R., and Corey, E. J., Molecular cloning of the human gene encoding lanosterol synthase from a liver cDNA library. Biochem. Biophys. Res. Com-mun., 213, 154-160 (1995).
    • (1995) Biochem. Biophys. Res. Com-Mun. , vol.213 , pp. 154-160
    • Baker, C.H.1    Matsuda, S.P.T.2    Liu, D.R.3    Corey, E.J.4
  • 14
    • 0029944635 scopus 로고    scopus 로고
    • Molecular cloning of a Schizosaccharomycespombe cDNA encoding lanosterol synthase and investigation of conserved tryptophan residues
    • Corey, E. J., Matsuda, S. P. T., Baker, C. H., Ting, A. Y., and Cheng, H., Molecular cloning of a Schizosaccharomycespombe cDNA encoding lanosterol synthase and investigation of conserved tryptophan residues. Biochem. Biophys. Res. Commun., 219, 327-331 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 327-331
    • Corey, E.J.1    Matsuda, S.P.T.2    Baker, C.H.3    Ting, A.Y.4    Cheng, H.5
  • 15
    • 0028280613 scopus 로고
    • The possible role of a repetitive amino acid motif in evolution of triterpenoid cyclases
    • Poralla, K., The possible role of a repetitive amino acid motif in evolution of triterpenoid cyclases. Bioorg. Med. Chem. Lett., 4, 285-290 (1994).
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 285-290
    • Poralla, K.1
  • 16
    • 37049084450 scopus 로고
    • Substitution of the methyl groups with ethyl groups at C-10 and C-15 of 2,3-ox-idosqualene halts the enzymatic reaction of oxidosqualene-lanosterol cyclase at the monocyclic ring stage
    • Hoshino, T., Ishibashi, E., and Kaneko, K., Substitution of the methyl groups with ethyl groups at C-10 and C-15 of 2,3-ox-idosqualene halts the enzymatic reaction of oxidosqualene-lanosterol cyclase at the monocyclic ring stage. J. Chem. Soc. Chem. Commun., 2401-2402 (1995).
    • (1995) J. Chem. Soc. Chem. Commun. , pp. 2401-2402
    • Hoshino, T.1    Ishibashi, E.2    Kaneko, K.3
  • 17
    • 21844478741 scopus 로고    scopus 로고
    • Further evidence that the polycycli-zation 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 polycycli-zation 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
  • 18
    • 0033591019 scopus 로고    scopus 로고
    • The cyclization mechanism of squa-lene 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 squa-lene 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
  • 19
    • 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
  • 20
    • 0031992366 scopus 로고    scopus 로고
    • Overexpression of squa-lene-hopene cyclase by the pET vector in Escherichia coli and first identification of tryptophan and aspartic acid residues inside the QW motif as active sites
    • Sato, T., Kanai, Y., and Hoshino, T., Overexpression of squa-lene-hopene cyclase by the pET vector in Escherichia coli and first identification of tryptophan and aspartic acid residues inside 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
  • 21
    • 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
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0030934889 scopus 로고    scopus 로고
    • Methodology for the preparation of pure recombinant S. Cerevisiae lanosterol synthase using a baculovi-rus expression system. Evidence that oxirane cleavage and A-ring formation are concerted in the biosynthesis of lanosterol from 2,3-oxidosqualene
    • Corey, E. J., Cheng, H., Baker, C. H., Matsuda, S. P. T., Li, D., and Song, X., Methodology for the preparation of pure recombinant S. cerevisiae lanosterol synthase using a baculovi-rus expression system. Evidence that oxirane cleavage and A-ring formation are concerted in the biosynthesis of lanosterol from 2,3-oxidosqualene. J. Am. Chem. Soc., 119, 1277-1288 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1277-1288
    • Corey, E.J.1    Cheng, H.2    Baker, C.H.3    Matsuda, S.P.T.4    Li, D.5    Song, X.6
  • 25
    • 0030984243 scopus 로고    scopus 로고
    • Studies on the substrate binding segments and catalytic action of lanosterol synthase. Affinity labeling with car-bocations derived from mechanism-based analogs of 2,3-ox-idosqualene and site-directed mutagenesis probes
    • Corey, E. J., Cheng, H., Baker, C. H., Matsuda, S. P. T., Li, D., and Song, X., Studies on the substrate binding segments and catalytic action of lanosterol synthase. Affinity labeling with car-bocations derived from mechanism-based analogs of 2,3-ox-idosqualene and site-directed mutagenesis probes. J. Am. Chem. Soc., 119, 1289-1296 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1289-1296
    • Corey, E.J.1    Cheng, H.2    Baker, C.H.3    Matsuda, S.P.T.4    Li, D.5    Song, X.6
  • 26
    • 0027979831 scopus 로고
    • Active site mapping of affinity-labeled rat oxidosqualene cyclase
    • Abe, I., and Prestwich, G. D., Active site mapping of affinity-labeled rat oxidosqualene cyclase. J. Biol. Chem., 269, 802-804 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 802-804
    • Abe, I.1    Prestwich, G.D.2
  • 27
    • 0028925271 scopus 로고
    • Identification of the active site of vertebrate oxidosqualene cyclase
    • Abe, I., and Prestwich, G. D., Identification of the active site of vertebrate oxidosqualene cyclase. Lipids, 30, 231-234 (1995).
    • (1995) Lipids , vol.30 , pp. 231-234
    • Abe, I.1    Prestwich, G.D.2
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0023200066 scopus 로고
    • Rate enhancement of biomimetic polyene cyclizations by a cation-stabilizing auxiliary
    • Johnson, W. S., Lindell, S. D., and Steele, J., Rate enhancement of biomimetic polyene cyclizations by a cation-stabilizing auxiliary. J. Am. Chem. Soc., 109, 5852-5853 (1987).
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5852-5853
    • Johnson, W.S.1    Lindell, S.D.2    Steele, J.3
  • 31
    • 0030043489 scopus 로고    scopus 로고
    • Cation-7t interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. A., Cation-7t interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science, 271,163-168 (1996).
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 33
    • 0033533760 scopus 로고    scopus 로고
    • Functional analysis of phenylalanine 365 in hopene synthase, a conserved amino acid in the families of squalene and oxidosqualene cyclases
    • Hoshino, T., and Sato, T., Functional analysis of phenylalanine 365 in hopene synthase, a conserved amino acid in the families of squalene and oxidosqualene cyclases, J. Chem. Soc. Chem. Commun., 2005-2006 (1999).
    • (1999) J. Chem. Soc. Chem. Commun. , pp. 2005-2006
    • Hoshino, T.1    Sato, T.2
  • 34
    • 0033218286 scopus 로고    scopus 로고
    • New cyclization mechanism of squalene: A ring expansion step of the five-membered C-ring intermediate in hopene biosynthesis
    • Hoshino, T., Kouda, M., Abe, T., and Ohashi, S., New cyclization mechanism of squalene: a ring expansion step of the five-membered C-ring intermediate in hopene biosynthesis. Biosci. Biotechnol. Biochem., 63, 2038-2041 (1999).
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 2038-2041
    • Hoshino, T.1    Kouda, M.2    Abe, T.3    Ohashi, S.4
  • 35
    • 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
  • 36
    • 0029928923 scopus 로고    scopus 로고
    • Trichodiene synthase. Enzymatic formation of multiple sesquiterpenes by alteration of the cyclase active site
    • Cane, D. E., and Xue, Q., Trichodiene synthase. Enzymatic formation of multiple sesquiterpenes by alteration of the cyclase active site. J. Am. Chem. Soc., 118, 1563-1564 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1563-1564
    • Cane, D.E.1    Xue, Q.2
  • 37
    • 0029836353 scopus 로고    scopus 로고
    • Enzymatic formation of isochamigrene, a novel sesquiterpene, by alteration of the aspartate-rich region of trichodiene synthase
    • Cane, D. E., Xue, Q., VanEpp, J. E., and Tsantrizos, Y. S., Enzymatic formation of isochamigrene, a novel sesquiterpene, by alteration of the aspartate-rich region of trichodiene synthase. J. Am. Chem. Soc., 118, 8499-8500 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8499-8500
    • Cane, D.E.1    Xue, Q.2    Vanepp, J.E.3    Tsantrizos, Y.S.4
  • 38
    • 0033515090 scopus 로고    scopus 로고
    • Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel “unnatural” natural products
    • McDaniel, R., Thamchaipenet, A., Gustafsson, C., Fu, H., Betlach, M., Betlach, M., and Ashley, G., Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel “unnatural” natural products. Proc. Natl. Acad. Sci. USA, 96, 1846-1851 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1846-1851
    • Mc Daniel, R.1    Thamchaipenet, A.2    Gustafsson, C.3    Fu, H.4    Betlach, M.5    Betlach, M.6    Ashley, G.7
  • 39
    • 0028520249 scopus 로고
    • The Arabidopsis GA1 locus encodes the cyclase erfi-kaurene synthase A of gibberellin biosynthesis
    • Sun, T.-P., and Kamiya, Y., The Arabidopsis GA1 locus encodes the cyclase erfi-kaurene synthase A of gibberellin biosynthesis. Plant Cell, 6, 1509-1518 (1994).
    • (1994) Plant Cell , vol.6 , pp. 1509-1518
    • Sun, T.-P.1    Kamiya, Y.2
  • 41
    • 0031106238 scopus 로고    scopus 로고
    • The LS locus of pea encodes the gibberellin biosynthesis enzyme e/zf-kaurene synthase A
    • Ait-Ali, T., Swain, S. M., Reid, J. B., Sun, T.-P., and Kamiya, Y., The LS locus of pea encodes the gibberellin biosynthesis enzyme e/zf-kaurene synthase A. Plant J., 11, 443-454 (1997).
    • (1997) Plant J. , vol.11 , pp. 443-454
    • Ait-Ali, T.1    Swain, S.M.2    Reid, J.B.3    Sun, T.-P.4    Kamiya, Y.5
  • 42
    • 0031717221 scopus 로고    scopus 로고
    • Gibberellin biosynthesis in Gibberella fujikurov. Cloning and characterization of the copalyl diphosphate synthase gene
    • Tudzynski, B., Kawaide, H., and Kamiya, Y., Gibberellin biosynthesis in Gibberella fujikurov. cloning and characterization of the copalyl diphosphate synthase gene. Curr. Genet., 34, 234-240 (1998).
    • (1998) Curr. Genet. , vol.34 , pp. 234-240
    • Tudzynski, B.1    Kawaide, H.2    Kamiya, Y.3
  • 43
    • 0032253618 scopus 로고    scopus 로고
    • The first step of gibberellin biosynthesis in pumpkin is catalyzed by at least two copalyl diphosphate synthases encoded by differentially regulated genes
    • Smith, M. W., Yamaguchi, S., Ait-Ali, T., and Kamiya, Y., The first step of gibberellin biosynthesis in pumpkin is catalyzed by at least two copalyl diphosphate synthases encoded by differentially regulated genes. Plant Physiol., 118, 1411-1419 (1998).
    • (1998) Plant Physiol. , vol.118 , pp. 1411-1419
    • Smith, M.W.1    Yamaguchi, S.2    Ait-Ali, T.3    Kamiya, Y.4
  • 44
    • 0000828106 scopus 로고    scopus 로고
    • Abietadiene synthase from grand fir (Abies grandis)
    • Vogel, B. S., Wildung, M. R., Vogel, G., and Croteau, R., Abietadiene synthase from grand fir (Abies grandis). J. Biol. Chem., 271, 23262-23268 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 23262-23268
    • Vogel, B.S.1    Wildung, M.R.2    Vogel, G.3    Croteau, R.4
  • 45
    • 0030826498 scopus 로고    scopus 로고
    • Enf-Kaurene synthase from the fungus Phaeosphaeria sp. L487
    • Kawaide, H., Imai, R., Sassa, T., and Kamiya, Y., enf-Kaurene synthase from the fungus Phaeosphaeria sp. L487. J. Biol. Chem., 272, 21706-21712 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 21706-21712
    • Kawaide, H.1    Imai, R.2    Sassa, T.3    Kamiya, Y.4


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