about
β-Amyrin biosynthesis: catalytic mechanism and substrate recognition.Euphorbia tirucalli β-amyrin cyclase: Trp612 and Tyr736 π-electrons participate in a cation-π interaction with the transient cation and a CH-π interaction with Leu734, respectively.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.β-Amyrin synthase from Euphorbia tirucalli L. functional analyses of the highly conserved aromatic residues Phe413, Tyr259 and Trp257 disclose the importance of the appropriate steric bulk, and cation-π and CH-π interactions for the efficient catalyChemical structure of cichorinotoxin, a cyclic lipodepsipeptide that is produced by and causes varnish spots on lettuceSqualene-Hopene Cyclase: Mechanistic Insights into the Polycyclization Cascades of Squalene Analogs Bearing Ethyl and Hydroxymethyl Groups at the C-2 and C-23 PositionsAlicyclobacillus acidocaldarius Squalene-Hopene Cyclase: The Critical Role of Steric Bulk at Ala306 and the First Enzymatic Synthesis of Epoxydammarane from 2,3-OxidosqualeneOryza sativa Parkeol Cyclase: Changes in the Substrate-Folding Conformation and the Deprotonation Sites on Mutation at Tyr257: Importance of the Hydroxy Group and Steric Bulk
P50
Q39179028-D660A2B0-21C2-4880-97EC-2D843BED1890Q47320885-5C19FFDF-CCB1-4EC9-9502-DC5861750C28Q47850360-AA6EE347-2BB1-47DF-944A-B29C844E0D67Q48165187-96D455A7-F71B-43BB-B577-897F4DF7FA65Q64235147-EE0819D9-285C-4F3C-BD6B-29485CF80CF3Q88585858-D31785AC-3C35-4804-A1D4-B74CBD493993Q89132927-C10DA951-7BC5-41EC-B559-050ED0388726Q92626287-3618DD26-8F26-4335-B664-ABB4BF14CF9E
P50
description
researcher
@en
name
Tsutomu Hoshino
@en
type
label
Tsutomu Hoshino
@en
prefLabel
Tsutomu Hoshino
@en
P31
P496
0000-0002-8484-2752