A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis

A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis

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http://www.wikidata.org/entity/Q27642536
Fluorescence spectroscopy approaches for the development of a real-time organophosphate detection system using an enzymatic sensorHow the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysisCloning, expression and characterization of a halotolerant esterase from a marine bacterium Pelagibacterium halotolerans B2T.Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase familyStructural insights into the substrate specificity of two esterases from the thermophilic Rhizomucor miehei.A Novel Subfamily Esterase with a Homoserine Transacetylase-like Fold but No Transferase Activity.The first description of a hormone-sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase.A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2.The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Thermogutta terrifontis Reveals an Open Active Site Due to a Minimal 'Cap' Domain.Conserved tyrosine 182 residue in hyperthermophilic esterase EstE1 plays a critical role in stabilizing the active site.Special Rhodococcus sp. CR-53 esterase Est4 contains a GGG(A)X-oxyanion hole conferring activity for the kinetic resolution of tertiary alcohols.Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation.
P2860

A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis

Item
http://www.wikidata.org/entity/Q27642536
description
2004 nî lūn-bûn
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2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
A substrate-induced switch in ...... evidences and structural basis
@ast
A substrate-induced switch in ...... evidences and structural basis
@en
A substrate-induced switch in ...... evidences and structural basis
@nl
type
label
A substrate-induced switch in ...... evidences and structural basis
@ast
A substrate-induced switch in ...... evidences and structural basis
@en
A substrate-induced switch in ...... evidences and structural basis
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prefLabel
A substrate-induced switch in ...... evidences and structural basis
@ast
A substrate-induced switch in ...... evidences and structural basis
@en
A substrate-induced switch in ...... evidences and structural basis
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P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
A substrate-induced switch in ...... evidences and structural basis
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P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698