(en) Yi Feng Zheng, Ikuro Abe et Glenn D. Prestwich, « Inhibition Kinetics and Affinity Labeling of Bacterial Squalene:Hopene Cyclase by Thia-Substituted Analogues of 2,3-Oxidosqualene », Biochemistry, vol. 37, no 17, , p. 5981-5987 (PMID9558334, DOI10.1021/bi9727343, lire en ligne)
(en) K. U. Wendt, A. Lenhart et G. E. Schulz, « The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution. », Journal of Molecular Biology, vol. 286, no 1, , p. 175-187 (PMID9931258, DOI10.1006/jmbi.1998.2470, lire en ligne)
(en) Tsutomu Hoshino et Tsutomu Sato, « Squalene–hopene cyclase: catalytic mechanism and substrate recognition », Chemical Communications, no 4, , p. 291-301 (PMID12120044, DOI10.1039/B108995c, lire en ligne)
(en) Tsutomu Hoshino, Schin-ichi Nakano, Tomohiro Kondo, Tsutomu Sato et Aya Miyoshi, « Squalene–hopene cyclase: final deprotonation reaction, conformational analysis for the cyclization of (3R,S)-2,3-oxidosqualene and further evidence for the requirement of an isopropylidene moiety both for initiation of the polycyclization cascade and for the formation of the 5-membered E-ring », Organic & Biomolecular Chemistry, vol. 2, no 10, , p. 1456-1470 (PMID15136801, DOI10.1039/B401172d, lire en ligne)
(en) Tsutomu Sato, Masanori Kouda et Tsutomu Hoshino, « Site-directed Mutagenesis Experiments on the Putative Deprotonation Site of Squalene-hopene Cyclase from Alicyclobacillus acidocaldarius », Bioscience, Biotechnology, and Biochemistry, vol. 68, no 3, , p. 728-738 (PMID15056909, DOI10.1271/bbb.68.728, lire en ligne)
(en) Dirk J. Reinert, Gianni Balliano et Georg E. Schulz, « Conversion of Squalene to the Pentacarbocyclic Hopene », Chemistry & Biology, vol. 11, no 1, , p. 121-126 (PMID15113001, DOI10.1016/j.chembiol.2003.12.013)
(en) Ann Pearson, Meytal Budin et Jochen J. Brocks, « Phylogenetic and biochemical evidence for sterol synthesis in the bacterium Gemmata obscuriglobus », Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no 26, , p. 15352-15357 (PMID14660793, PMCID307571, DOI10.1073/pnas.2536559100, lire en ligne)
(en) Brigitte Seckler et Karl Poralla, « Characterization and partial purification of squalene-hopene cyclase from Bacillus acidocaldarius », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 881, no 3, , p. 356-363 (DOI10.1016/0304-4165(86)90027-9, lire en ligne)
(en) Hermann Sahm, Michel Rohmer, Stephanie Bringer-Meyer, Georg A. Sprenger et Roland Welle, « Biochemistry and Physiology of Hopanoids in Bacteria », Advances in Microbial Physiology, vol. 35, , p. 247-273 (PMID8310881, DOI10.1016/S0065-2911(08)60100-9, lire en ligne)
(en) M Rohmer, P Bouvier et G Ourisson, « Molecular evolution of biomembranes: structural equivalents and phylogenetic precursors of sterols », Proceedings of the National Academy of Sciences of the United States of America, vol. 76, no 2, , p. 847-851 (PMID284408, PMCID383070, DOI10.1073/pnas.76.2.847, lire en ligne)
(en) E. J. Corey, S. P. Matsuda et B. Bartel, « 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 », Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no 24, , p. 11628-11632 (PMID7505443, PMCID48037, DOI10.1073/pnas.90.24.11628, lire en ligne)
(en) Yi Feng Zheng, Ikuro Abe et Glenn D. Prestwich, « Inhibition Kinetics and Affinity Labeling of Bacterial Squalene:Hopene Cyclase by Thia-Substituted Analogues of 2,3-Oxidosqualene », Biochemistry, vol. 37, no 17, , p. 5981-5987 (PMID9558334, DOI10.1021/bi9727343, lire en ligne)
(en) Yang Gao, Richard B. Honzatko et Reuben J. Peters, « Terpenoid synthase structures: a so far incomplete view of complex catalysis », Natural Product Reports, vol. 29, no 10, , p. 1153-1175 (PMID22907771, PMCID3448952, DOI10.1039/C2NP20059G, lire en ligne)
(en) Corinna Feil, Roderich Süssmuth, Günther Jung et Karl Poralla, « Site‐Directed Mutagenesis of Putative Active‐Site Residues in Squalene‐Hopene Cyclase », European Journal of Biochemistry, vol. 242, no 1, , p. 51-55 (PMID8954152, DOI10.1111/j.1432-1033.1996.0051r.x, lire en ligne)
(en) K. U. Wendt, A. Lenhart et G. E. Schulz, « The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution. », Journal of Molecular Biology, vol. 286, no 1, , p. 175-187 (PMID9931258, DOI10.1006/jmbi.1998.2470, lire en ligne)
(en) Tsutomu Hoshino et Tsutomu Sato, « Squalene–hopene cyclase: catalytic mechanism and substrate recognition », Chemical Communications, no 4, , p. 291-301 (PMID12120044, DOI10.1039/B108995c, lire en ligne)
(en) Tsutomu Hoshino, Schin-ichi Nakano, Tomohiro Kondo, Tsutomu Sato et Aya Miyoshi, « Squalene–hopene cyclase: final deprotonation reaction, conformational analysis for the cyclization of (3R,S)-2,3-oxidosqualene and further evidence for the requirement of an isopropylidene moiety both for initiation of the polycyclization cascade and for the formation of the 5-membered E-ring », Organic & Biomolecular Chemistry, vol. 2, no 10, , p. 1456-1470 (PMID15136801, DOI10.1039/B401172d, lire en ligne)
(en) Tsutomu Sato, Masanori Kouda et Tsutomu Hoshino, « Site-directed Mutagenesis Experiments on the Putative Deprotonation Site of Squalene-hopene Cyclase from Alicyclobacillus acidocaldarius », Bioscience, Biotechnology, and Biochemistry, vol. 68, no 3, , p. 728-738 (PMID15056909, DOI10.1271/bbb.68.728, lire en ligne)
(en) Dirk J. Reinert, Gianni Balliano et Georg E. Schulz, « Conversion of Squalene to the Pentacarbocyclic Hopene », Chemistry & Biology, vol. 11, no 1, , p. 121-126 (PMID15113001, DOI10.1016/j.chembiol.2003.12.013)
(en) Ann Pearson, Meytal Budin et Jochen J. Brocks, « Phylogenetic and biochemical evidence for sterol synthesis in the bacterium Gemmata obscuriglobus », Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no 26, , p. 15352-15357 (PMID14660793, PMCID307571, DOI10.1073/pnas.2536559100, lire en ligne)
(en) Hermann Sahm, Michel Rohmer, Stephanie Bringer-Meyer, Georg A. Sprenger et Roland Welle, « Biochemistry and Physiology of Hopanoids in Bacteria », Advances in Microbial Physiology, vol. 35, , p. 247-273 (PMID8310881, DOI10.1016/S0065-2911(08)60100-9, lire en ligne)
(en) M Rohmer, P Bouvier et G Ourisson, « Molecular evolution of biomembranes: structural equivalents and phylogenetic precursors of sterols », Proceedings of the National Academy of Sciences of the United States of America, vol. 76, no 2, , p. 847-851 (PMID284408, PMCID383070, DOI10.1073/pnas.76.2.847, lire en ligne)
(en) E. J. Corey, S. P. Matsuda et B. Bartel, « 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 », Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no 24, , p. 11628-11632 (PMID7505443, PMCID48037, DOI10.1073/pnas.90.24.11628, lire en ligne)
(en) Yi Feng Zheng, Ikuro Abe et Glenn D. Prestwich, « Inhibition Kinetics and Affinity Labeling of Bacterial Squalene:Hopene Cyclase by Thia-Substituted Analogues of 2,3-Oxidosqualene », Biochemistry, vol. 37, no 17, , p. 5981-5987 (PMID9558334, DOI10.1021/bi9727343, lire en ligne)
(en) Yang Gao, Richard B. Honzatko et Reuben J. Peters, « Terpenoid synthase structures: a so far incomplete view of complex catalysis », Natural Product Reports, vol. 29, no 10, , p. 1153-1175 (PMID22907771, PMCID3448952, DOI10.1039/C2NP20059G, lire en ligne)
(en) Corinna Feil, Roderich Süssmuth, Günther Jung et Karl Poralla, « Site‐Directed Mutagenesis of Putative Active‐Site Residues in Squalene‐Hopene Cyclase », European Journal of Biochemistry, vol. 242, no 1, , p. 51-55 (PMID8954152, DOI10.1111/j.1432-1033.1996.0051r.x, lire en ligne)
pnas.org
(en) Ann Pearson, Meytal Budin et Jochen J. Brocks, « Phylogenetic and biochemical evidence for sterol synthesis in the bacterium Gemmata obscuriglobus », Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no 26, , p. 15352-15357 (PMID14660793, PMCID307571, DOI10.1073/pnas.2536559100, lire en ligne)
(en) M Rohmer, P Bouvier et G Ourisson, « Molecular evolution of biomembranes: structural equivalents and phylogenetic precursors of sterols », Proceedings of the National Academy of Sciences of the United States of America, vol. 76, no 2, , p. 847-851 (PMID284408, PMCID383070, DOI10.1073/pnas.76.2.847, lire en ligne)
(en) E. J. Corey, S. P. Matsuda et B. Bartel, « 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 », Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no 24, , p. 11628-11632 (PMID7505443, PMCID48037, DOI10.1073/pnas.90.24.11628, lire en ligne)
rsc.org
pubs.rsc.org
(en) Tsutomu Hoshino et Tsutomu Sato, « Squalene–hopene cyclase: catalytic mechanism and substrate recognition », Chemical Communications, no 4, , p. 291-301 (PMID12120044, DOI10.1039/B108995c, lire en ligne)
(en) Tsutomu Hoshino, Schin-ichi Nakano, Tomohiro Kondo, Tsutomu Sato et Aya Miyoshi, « Squalene–hopene cyclase: final deprotonation reaction, conformational analysis for the cyclization of (3R,S)-2,3-oxidosqualene and further evidence for the requirement of an isopropylidene moiety both for initiation of the polycyclization cascade and for the formation of the 5-membered E-ring », Organic & Biomolecular Chemistry, vol. 2, no 10, , p. 1456-1470 (PMID15136801, DOI10.1039/B401172d, lire en ligne)
(en) Yang Gao, Richard B. Honzatko et Reuben J. Peters, « Terpenoid synthase structures: a so far incomplete view of complex catalysis », Natural Product Reports, vol. 29, no 10, , p. 1153-1175 (PMID22907771, PMCID3448952, DOI10.1039/C2NP20059G, lire en ligne)
sciencedirect.com
(en) K. U. Wendt, A. Lenhart et G. E. Schulz, « The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution. », Journal of Molecular Biology, vol. 286, no 1, , p. 175-187 (PMID9931258, DOI10.1006/jmbi.1998.2470, lire en ligne)
(en) Brigitte Seckler et Karl Poralla, « Characterization and partial purification of squalene-hopene cyclase from Bacillus acidocaldarius », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 881, no 3, , p. 356-363 (DOI10.1016/0304-4165(86)90027-9, lire en ligne)
(en) Hermann Sahm, Michel Rohmer, Stephanie Bringer-Meyer, Georg A. Sprenger et Roland Welle, « Biochemistry and Physiology of Hopanoids in Bacteria », Advances in Microbial Physiology, vol. 35, , p. 247-273 (PMID8310881, DOI10.1016/S0065-2911(08)60100-9, lire en ligne)
(en) Tsutomu Sato, Masanori Kouda et Tsutomu Hoshino, « Site-directed Mutagenesis Experiments on the Putative Deprotonation Site of Squalene-hopene Cyclase from Alicyclobacillus acidocaldarius », Bioscience, Biotechnology, and Biochemistry, vol. 68, no 3, , p. 728-738 (PMID15056909, DOI10.1271/bbb.68.728, lire en ligne)
wiley.com
febs.onlinelibrary.wiley.com
(en) Corinna Feil, Roderich Süssmuth, Günther Jung et Karl Poralla, « Site‐Directed Mutagenesis of Putative Active‐Site Residues in Squalene‐Hopene Cyclase », European Journal of Biochemistry, vol. 242, no 1, , p. 51-55 (PMID8954152, DOI10.1111/j.1432-1033.1996.0051r.x, lire en ligne)
