Cation-pi interaction in the polyolefin cyclization cascade uncovered by incorporating unnatural amino acids into the catalytic sites of squalene cyclase.
about
Squalene-hopene cyclasesEnantioselective thiourea-catalyzed cationic polycyclizationsAttractive noncovalent interactions in asymmetric catalysis: links between enzymes and small molecule catalystsBiochemical evidence for the tyrosine involvement in cationic intermediate stabilization in mouse beta-carotene 15, 15'-monooxygenase.Cloning and characterization of oxidosqualene cyclases from Kalanchoe daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding friedelin and other triterpenoids.Terpenoid synthase structures: a so far incomplete view of complex catalysis.Unusually cyclized triterpenes: occurrence, biosynthesis and chemical synthesis.The cation-π interaction.Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology.β-Amyrin biosynthesis: catalytic mechanism and substrate recognition.Activation-independent cyclization of monoterpenoids.Comprehensive Structural Characterization of the Bacterial Homospermidine Synthase-an Essential Enzyme of the Polyamine Metabolism.Aromatic Interactions in Organocatalyst Design: Augmenting Selectivity Reversal in Iminium Ion Activation.Exploiting non-covalent π interactions for catalyst design.Entropy is key to the formation of pentacyclic terpenoids by enzyme-catalyzed polycyclization.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.The triterpene cyclase protein family: a systematic analysis.A cation-pi interaction discriminates among sodium channels that are either sensitive or resistant to tetrodotoxin block.Exploring water as building bricks in enzyme engineering.Biochemical characterization of the water-soluble squalene synthase from Methylococcus capsulatus and the functional analyses of its two DXXD(E)D motifs and the highly conserved aromatic amino acid residues.
P2860
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P2860
Cation-pi interaction in the polyolefin cyclization cascade uncovered by incorporating unnatural amino acids into the catalytic sites of squalene cyclase.
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@ast
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@en
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@nl
type
label
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@ast
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@en
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@nl
prefLabel
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@ast
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@en
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@nl
P2093
P50
P356
P1476
Cation-pi interaction in the p ...... tic sites of squalene cyclase.
@en
P2093
Hiroshi Hirota
Kazumasa Ohtake
Miwako Asanuma
Naoko Shinya
Noriko Morikubo
Tsutomu Hoshino
Yoriyuki Fukuda
P304
13184-13194
P356
10.1021/JA063358P
P407
P577
2006-10-01T00:00:00Z