Diversity of reaction characteristics of ...
Type de document :
Article dans une revue scientifique
URL permanente :
Titre :
Diversity of reaction characteristics of glucan branching enzymes and the fine structure of α-glucan from various sources
Auteur(s) :
Sawada, Takayuki [Auteur]
Akita University
Nakamura, Yasunori [Auteur]
Akita University
Ohdan, Takashi [Auteur]
Akita University
Saitoh, Asami [Auteur]
Akita University
Perigio B., Francisco Jr. [Auteur]
Akita University
Suzuki, Eiji [Auteur]
Akita University
Fujita, Naoko [Auteur]
Akita University
Shimonaga, Takahiro [Auteur]
Tokyo Metropolitan University [Tokyo] [TMU]
Fujiwara, Shoko [Auteur]
Tokyo Metropolitan University [Tokyo] [TMU]
Tsuzuki, Mikio [Auteur]
Tokyo Metropolitan University [Tokyo] [TMU]
Colleoni, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Ball, Steven [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Akita University
Nakamura, Yasunori [Auteur]
Akita University
Ohdan, Takashi [Auteur]
Akita University
Saitoh, Asami [Auteur]
Akita University
Perigio B., Francisco Jr. [Auteur]
Akita University
Suzuki, Eiji [Auteur]
Akita University
Fujita, Naoko [Auteur]
Akita University
Shimonaga, Takahiro [Auteur]
Tokyo Metropolitan University [Tokyo] [TMU]
Fujiwara, Shoko [Auteur]
Tokyo Metropolitan University [Tokyo] [TMU]
Tsuzuki, Mikio [Auteur]
Tokyo Metropolitan University [Tokyo] [TMU]
Colleoni, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Ball, Steven [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Titre de la revue :
Archives of biochemistry and biophysics
Numéro :
562
Pagination :
9-21
Date de publication :
2014-11
Mot(s)-clé(s) en anglais :
Glucan branching enzyme
Chain-length distribution
Phosphorylase limit dextrin
Amylopectin
Glycogen
Starch
Chain-length distribution
Phosphorylase limit dextrin
Amylopectin
Glycogen
Starch
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biochimie [q-bio.BM]
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biochimie [q-bio.BM]
Résumé en anglais : [en]
To investigate the functional properties of 10 α-glucan branching enzymes (BEs) from various sources, we determined the chain-length distribution of BE enzymatic products and their phosphorylase-limit dextrins (Φ-LD). All ...
Lire la suite >To investigate the functional properties of 10 α-glucan branching enzymes (BEs) from various sources, we determined the chain-length distribution of BE enzymatic products and their phosphorylase-limit dextrins (Φ-LD). All BEs could be classified into either of the three rice BE isozymes: OsBEI, OsBEIIa, or OsBEIIb. Escherichia coli BE (EcoBE) had the same enzymatic properties as OsBEI, while Synechococcus elongatus BE (ScoBE) and Chlorella kessleri BE (ChlBE) had BEIIb-type properties. Human BE (HosBE), yeast BE (SacBE), and two Porphyridium purpureum BEs (PopBE1 and PopBE2) exhibited the OsBEIIa-type properties. Analysis of chain-length profile of Φ-LD of the BE reaction products revealed that EcoBE, ScoBE, PopBE1, and PopBE2 preferred A-chains as acceptors, while OsBEIIb used B-chains more frequently than A-chains. Both EcoBE and ScoBE specifically formed the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The present results provide evidence for the first time that great variation exists as to the preference of BEs for their acceptor chain, either A-chain or B-chain. In addition, EcoBE and ScoBE recognize the location of branching points in their acceptor chain during their branching reaction. Nevertheless, no correlation exists between the primary structure of BE proteins and their enzymatic characteristics.Lire moins >
Lire la suite >To investigate the functional properties of 10 α-glucan branching enzymes (BEs) from various sources, we determined the chain-length distribution of BE enzymatic products and their phosphorylase-limit dextrins (Φ-LD). All BEs could be classified into either of the three rice BE isozymes: OsBEI, OsBEIIa, or OsBEIIb. Escherichia coli BE (EcoBE) had the same enzymatic properties as OsBEI, while Synechococcus elongatus BE (ScoBE) and Chlorella kessleri BE (ChlBE) had BEIIb-type properties. Human BE (HosBE), yeast BE (SacBE), and two Porphyridium purpureum BEs (PopBE1 and PopBE2) exhibited the OsBEIIa-type properties. Analysis of chain-length profile of Φ-LD of the BE reaction products revealed that EcoBE, ScoBE, PopBE1, and PopBE2 preferred A-chains as acceptors, while OsBEIIb used B-chains more frequently than A-chains. Both EcoBE and ScoBE specifically formed the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The present results provide evidence for the first time that great variation exists as to the preference of BEs for their acceptor chain, either A-chain or B-chain. In addition, EcoBE and ScoBE recognize the location of branching points in their acceptor chain during their branching reaction. Nevertheless, no correlation exists between the primary structure of BE proteins and their enzymatic characteristics.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Génétique microbienne
Date de dépôt :
2020-02-12T15:45:08Z
2021-02-26T10:28:47Z
2021-02-26T10:31:32Z
2021-02-26T10:28:47Z
2021-02-26T10:31:32Z