title: Diversity of reaction characteristics of glucan branching enzymes and the fine structure of α-glucan from various sources.
abstract: 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.
authors.affiliation: Faculty of Bioresource Sciences, Akita Prefectural University, 241-438 Kaidobata-Nishi, Shimoshinjo-Nakano, Akita 010-0195, Japan.
authors.forename: Takayuki
authors.initials: T
authors.lastname: Sawada
authors.affiliation: Faculty of Bioresource Sciences, Akita Prefectural University, 241-438 Kaidobata-Nishi, Shimoshinjo-Nakano, Akita 010-0195, Japan; Akita Natural Science Laboratory, 25-44 Oiwake-Nishi, Tennoh, Katagami, Akita 010-0101, Japan. Electronic address: nakayn@silver.plala.or.jp.
authors.forename: Yasunori
authors.initials: Y
authors.lastname: Nakamura
authors.affiliation: Faculty of Bioresource Sciences, Akita Prefectural University, 241-438 Kaidobata-Nishi, Shimoshinjo-Nakano, Akita 010-0195, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Ohdan
authors.affiliation: Faculty of Bioresource Sciences, Akita Prefectural University, 241-438 Kaidobata-Nishi, Shimoshinjo-Nakano, Akita 010-0195, Japan.
authors.forename: Asami
authors.initials: A
authors.lastname: Saitoh
authors.affiliation: Faculty of Bioresource Sciences, Akita Prefectural University, 241-438 Kaidobata-Nishi, Shimoshinjo-Nakano, Akita 010-0195, Japan.
authors.forename: Perigio B
authors.initials: PB
authors.lastname: Francisco
authors.affiliation: Faculty of Bioresource Sciences, Akita Prefectural University, 241-438 Kaidobata-Nishi, Shimoshinjo-Nakano, Akita 010-0195, Japan.
authors.forename: Eiji
authors.initials: E
authors.lastname: Suzuki
authors.affiliation: Faculty of Bioresource Sciences, Akita Prefectural University, 241-438 Kaidobata-Nishi, Shimoshinjo-Nakano, Akita 010-0195, Japan.
authors.forename: Naoko
authors.initials: N
authors.lastname: Fujita
authors.affiliation: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Horinouchi, Hachioji, Tokyo 192-0392, Japan.
authors.forename: Takahiro
authors.initials: T
authors.lastname: Shimonaga
authors.affiliation: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Horinouchi, Hachioji, Tokyo 192-0392, Japan.
authors.forename: Shoko
authors.initials: S
authors.lastname: Fujiwara
authors.affiliation: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Horinouchi, Hachioji, Tokyo 192-0392, Japan.
authors.forename: Mikio
authors.initials: M
authors.lastname: Tsuzuki
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Colleoni
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France.
authors.forename: Steven
authors.initials: S
authors.lastname: Ball
mesh_terms: D015061:1,4-alpha-Glucan Branching Enzyme / Q000737:chemistry*; D000687:Amylopectin / Q000737:chemistry; D002708:Chlorella / Q000201:enzymology; D003912:Dextrins / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology; D005658:Fungi / Q000201:enzymology; D005936:Glucans / Q000737:chemistry*; D006003:Glycogen / Q000737:chemistry; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry; D012275:Oryza / Q000201:enzymology; D006005:Phosphorylases / Q000737:chemistry; D010802:Phylogeny; D044665:Porphyridium / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry; D013045:Species Specificity; D013213:Starch / Q000737:chemistry; D046940:Synechococcus / Q000201:enzymology
chemical_list: D003912:Dextrins; D005936:Glucans; D007527:Isoenzymes; D011994:Recombinant Proteins; D013213:Starch; D006003:Glycogen; D000687:Amylopectin; D006005:Phosphorylases; D015061:1,4-alpha-Glucan Branching Enzyme
keywords: Amylopectin; Chain-length distribution; Glucan branching enzyme; Glycogen; Phosphorylase limit dextrin; Starch