title: 1,2-β-Oligoglucan phosphorylase from Listeria innocua.
abstract: We characterized recombinant Lin1839 protein (Lin1839r) belonging to glycoside hydrolase family 94 from Listeria innocua. Lin1839r catalyzed the synthesis of a series of 1,2-β-oligoglucans (Sopn: n denotes degree of polymerization) using sophorose (Sop2) as the acceptor and α-D-glucose 1-phosphate (Glc1P) as the donor. Lin1839r recognized glucose as a very weak acceptor substrate to form polymeric 1,2-β-glucan. The degree of polymerization of the 1,2-β-glucan gradually decreased with long-term incubation to generate a series of Sopns. Kinetic analysis of the phosphorolytic reaction towards sophorotriose revealed that Lin1839r followed a sequential Bi Bi mechanism. The kinetic parameters of the phosphorolysis of sophorotetraose and sophoropentaose were similar to those of sophorotriose, although the enzyme did not exhibit significant phosphorolytic activity on Sop2. These results indicate that the Lin1839 protein is a novel inverting phosphorylase that catalyzes reversible phosphorolysis of 1,2-β-glucan with a degree of polymerization of ≥3. We propose 1,2-β-oligoglucan: phosphate α-glucosyltransferase as the systematic name and 1,2-β-oligoglucan phosphorylase as the short name for this Lin1839 protein.
authors.affiliation: Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba, Japan; National Food Research Institute, National Agriculture and Food Research Organization, Tsukuba, Ibaraki, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Nakajima
authors.affiliation: Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba, Japan.
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Toyoizumi
authors.affiliation: Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba, Japan.
authors.forename: Koichi
authors.initials: K
authors.lastname: Abe
authors.affiliation: Graduate School of Science & Technology, Niigata University, Niigata, Niigata, Japan.
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Nakai
authors.affiliation: Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba, Japan.
authors.forename: Hayao
authors.initials: H
authors.lastname: Taguchi
authors.affiliation: National Food Research Institute, National Agriculture and Food Research Organization, Tsukuba, Ibaraki, Japan.
authors.forename: Motomitsu
authors.initials: M
authors.lastname: Kitaoka
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D007700:Kinetics; D008087:Listeria / Q000201:enzymology*; D006005:Phosphorylases / Q000378:metabolism*; D013379:Substrate Specificity; D047071:beta-Glucans / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D047071:beta-Glucans; C033744:beta-1,2-glucan; D006005:Phosphorylases