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Euphorbia tirucalli β-Amyrin Synthase: Critical Roles of Steric Sizes at Val483 and Met729 and the CH-π Interaction between Val483 and Trp534 for Catalytic Action

Autor: Yukari Aiba, Tsutomu Hoshino, Yukari Masukawa, Chika Nakada, Kazuya Nakagawa, Daichi Itoh

Publikováno v: ChemBioChem. 18:2145-2155

The functions of Val483, Trp534, and Met729 in Euphorbia tirucalli β-amyrin synthase were revealed by comparing the enzyme activities of site-directed mutants against that of the wild type. The Gly and Ala variants with a smaller bulk size at positi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eadad7d65ec52e0d94e8664e74fe35f8
https://doi.org/10.1002/cbic.201700368

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Strictly Conserved Residues in Euphorbia tirucalli β-Amyrin Cyclase: Trp612 Stabilizes Transient Cation through Cation-π Interaction and CH-π Interaction of Tyr736 with Leu734 Confers Robust Local Protein Architecture

Autor: Yukari Aiba, Tsutomu Hoshino, Yuri Terasawa, Takumi Watanabe, Chiaki Nakano

Publikováno v: Chembiochem : a European journal of chemical biology. 19(5)

The functions of Trp612, Leu734, and Tyr736 of Euphorbia tirucalli β-amyrin synthase were examined. The aliphatic variants (Ala, Val, Met) of Trp612 showed almost no activity, but the aromatic variants exhibited high activities: 12.5 % of the wild-t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::903e233088944d6985aa25048112d6bb
https://pubmed.ncbi.nlm.nih.gov/29214725

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