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- Control of the 1,2-rearrangement process by oxidosqualene cyclases during triterpene biosynthesis. Shohei Takase, Yusuke Saga, Nozomi Kurihara, Shingo Naraki, Kenta Kuze, Genki Nakata, Takeshi Araki, Tetsuo Kushiro
, Org. Biomol. Chem.
, 2015
, 13
, 7331
- Mutagenesis approaches to deduce structure–function relationships in terpene synthases. Michael J. R. Segura, Beth E. Jackson, Seiichi P. T. Matsuda
, Nat. Prod. Rep.
, 2003
, 20
, 304
- Site-directed mutagenesis and substrate compatibility to reveal the structure–function relationships of plant oxidosqualene cyclases. Kuan Chen, Meng Zhang, Min Ye, Xue Qiao
, Nat. Prod. Rep.
, 2021
, 38
, 2261
- The protosteryl and dammarenyl cation dichotomy in polycyclic triterpene biosynthesis revisited: has this ‘rule’ finally been broken?. Michael J. Stephenson, Robert A. Field, Anne Osbourn
, Nat. Prod. Rep.
, 2019
, 36
, 1044
- β-Amyrin biosynthesis: catalytic mechanism and substrate recognition. Tsutomu Hoshino
, Org. Biomol. Chem.
, 2017
, 15
, 2869
- Enzymatic synthesis of cyclic triterpenes. Ikuro Abe
, Nat. Prod. Rep.
, 2007
, 24
, 1311
- The biosynthesis of cucurbitacin B. J. Malcolm Zander, Donald C. Wigfield
, J. Chem. Soc. D
, 1970
, 1599
- Protein engineering of oxidosqualene-lanosterol cyclase into triterpene monocyclase. Cheng-Hsiang Chang, Hao-Yu Wen, Wen-Shiang Shie, Ching-Ting Lu, Meng-Erh Li, Yuan-Ting Liu, Wen-Hsuan Li, Tung-Kung Wu
, Org. Biomol. Chem.
, 2013
, 11
, 4214
- Investigations on the biosynthesis of steroids and terpenoids. Part VI. The sterols of yeast. D. H. R. Barton, U. M. Kempe, D. A. Widdowson
, J. Chem. Soc., Perkin Trans. 1
, 1972
, 513
- β-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the π-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade. Ryousuke Ito, Yukari Masukawa, Chika Nakada, Kanako Amari, Chiaki Nakano, Tsutomu Hoshino
, Org. Biomol. Chem.
, 2014
, 12
, 3836