1,2-β-Oligoglucan phosphorylase from Listeria innocua.

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 (...

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Autores principales:	Masahiro Nakajima, Hiroyuki Toyoizumi, Koichi Abe, Hiroyuki Nakai, Hayao Taguchi, Motomitsu Kitaoka
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/66e46c71f2f14919ac97e4ae057ea6be
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spelling	oai:doaj.org-article:66e46c71f2f14919ac97e4ae057ea6be2021-11-18T08:27:13Z1,2-β-Oligoglucan phosphorylase from Listeria innocua.1932-620310.1371/journal.pone.0092353https://doaj.org/article/66e46c71f2f14919ac97e4ae057ea6be2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24647662/?tool=EBIhttps://doaj.org/toc/1932-6203We 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.Masahiro NakajimaHiroyuki ToyoizumiKoichi AbeHiroyuki NakaiHayao TaguchiMotomitsu KitaokaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 3, p e92353 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Masahiro Nakajima Hiroyuki Toyoizumi Koichi Abe Hiroyuki Nakai Hayao Taguchi Motomitsu Kitaoka 1,2-β-Oligoglucan phosphorylase from Listeria innocua.
description	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.
format	article
author	Masahiro Nakajima Hiroyuki Toyoizumi Koichi Abe Hiroyuki Nakai Hayao Taguchi Motomitsu Kitaoka
author_facet	Masahiro Nakajima Hiroyuki Toyoizumi Koichi Abe Hiroyuki Nakai Hayao Taguchi Motomitsu Kitaoka
author_sort	Masahiro Nakajima
title	1,2-β-Oligoglucan phosphorylase from Listeria innocua.
title_short	1,2-β-Oligoglucan phosphorylase from Listeria innocua.
title_full	1,2-β-Oligoglucan phosphorylase from Listeria innocua.
title_fullStr	1,2-β-Oligoglucan phosphorylase from Listeria innocua.
title_full_unstemmed	1,2-β-Oligoglucan phosphorylase from Listeria innocua.
title_sort	1,2-β-oligoglucan phosphorylase from listeria innocua.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/66e46c71f2f14919ac97e4ae057ea6be
work_keys_str_mv	AT masahironakajima 12boligoglucanphosphorylasefromlisteriainnocua AT hiroyukitoyoizumi 12boligoglucanphosphorylasefromlisteriainnocua AT koichiabe 12boligoglucanphosphorylasefromlisteriainnocua AT hiroyukinakai 12boligoglucanphosphorylasefromlisteriainnocua AT hayaotaguchi 12boligoglucanphosphorylasefromlisteriainnocua AT motomitsukitaoka 12boligoglucanphosphorylasefromlisteriainnocua
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1,2-β-Oligoglucan phosphorylase from Listeria innocua.

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