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Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site

Carbohydrate esterase catalyzes the de‐ or de‐‐acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from . Here, we prepared the recombinant catalytic do... Full description

Journal Title: FEBS Letters 08 May 2015, Vol.589(11), pp.1200-1206
Main Author: Watanabe, Masahiro
Other Authors: Fukada, Harumi , Inoue, Hiroyuki , Ishikawa, Kazuhiko
Format: Electronic Article Electronic Article
Language:
Subjects:
Dsc
Pna
Pnb
Pno
ID: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2015.03.020
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recordid: wj10.1016/j.febslet.2015.03.020
title: Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site
format: Article
creator:
  • Watanabe, Masahiro
  • Fukada, Harumi
  • Inoue, Hiroyuki
  • Ishikawa, Kazuhiko
subjects:
  • Tcae206
  • The Catalytic Domain Of Acetylesterase From Talaromyces Cellulolyticus
  • Dsc
  • Differential Scanning Calorimetry
  • Pna
  • P -Nitrophenyl Acetate
  • Pnb
  • P -Nitrophenyl Butyrate
  • Pno
  • P -Nitrophenyl Octanoate
  • Biomass
  • Carbohydrate Esterase
  • Catalytic Triad
  • Disulfide Bond
  • Saccharification
  • Xylanase
ispartof: FEBS Letters, 08 May 2015, Vol.589(11), pp.1200-1206
description: Carbohydrate esterase catalyzes the de‐ or de‐‐acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from . Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5 Å resolution. From the structural analysis, it was elucidated that a n‐octyl‐β‐‐glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site‐directed mutagenesis showed that the N‐terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme. The crystal structure of TcAE206 was determined at 1.5Å resolution. TcAE resembles a bacterial CE3 family but has a unique SS bond near the active site. A SS bond (Cys16–Cys47) plays an important role in protein folding and activity.
language:
source:
identifier: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2015.03.020
fulltext: fulltext
issn:
  • 0014-5793
  • 00145793
  • 1873-3468
  • 18733468
url: Link


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titleCrystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site
creatorWatanabe, Masahiro ; Fukada, Harumi ; Inoue, Hiroyuki ; Ishikawa, Kazuhiko
ispartofFEBS Letters, 08 May 2015, Vol.589(11), pp.1200-1206
identifier
subjectTcae206 ; The Catalytic Domain Of Acetylesterase From Talaromyces Cellulolyticus ; Dsc ; Differential Scanning Calorimetry ; Pna ; P -Nitrophenyl Acetate ; Pnb ; P -Nitrophenyl Butyrate ; Pno ; P -Nitrophenyl Octanoate ; Biomass ; Carbohydrate Esterase ; Catalytic Triad ; Disulfide Bond ; Saccharification ; Xylanase
descriptionCarbohydrate esterase catalyzes the de‐ or de‐‐acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from . Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5 Å resolution. From the structural analysis, it was elucidated that a n‐octyl‐β‐‐glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site‐directed mutagenesis showed that the N‐terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme. The crystal structure of TcAE206 was determined at 1.5Å resolution. TcAE resembles a bacterial CE3 family but has a unique SS bond near the active site. A SS bond (Cys16–Cys47) plays an important role in protein folding and activity.
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titleCrystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site
descriptionCarbohydrate esterase catalyzes the de‐ or de‐‐acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from . Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5 Å resolution. From the structural analysis, it was elucidated that a n‐octyl‐β‐‐glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site‐directed mutagenesis showed that the N‐terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme. The crystal structure of TcAE206 was determined at 1.5Å resolution. TcAE resembles a bacterial CE3 family but has a unique SS bond near the active site. A SS bond (Cys16–Cys47) plays an important role in protein folding and activity.
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titleCrystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site
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abstractCarbohydrate esterase catalyzes the de‐ or de‐‐acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from . Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5 Å resolution. From the structural analysis, it was elucidated that a n‐octyl‐β‐‐glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site‐directed mutagenesis showed that the N‐terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme. The crystal structure of TcAE206 was determined at 1.5Å resolution. TcAE resembles a bacterial CE3 family but has a unique SS bond near the active site. A SS bond (Cys16–Cys47) plays an important role in protein folding and activity.
doi10.1016/j.febslet.2015.03.020
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pages1200-1206
date2015-05-08