ArticlePloS one2014
1,2-β-Oligoglucan phosphorylase from Listeria innocua.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 49 citations in OpenAlex.
- A β-1,2-glucan-associated glycoside hydrolase family 1 β-glucosidase from Streptomyces griseus.Protein science : a publication of the Protein Society · 2025Article
- New glycoside hydrolase families of β-1,2-glucanases.Protein science : a publication of the Protein Society · 2025Article
- Enzymes that catalyze cyclization of β-1,2-glucans.Applied microbiology and biotechnology · 2025Review
- Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans.Nature communications · 2024Article
- Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase.Applied microbiology and biotechnology · 2024Article
- Identification of enzymatic functions of osmo-regulated periplasmic glucan biosynthesis proteins from Escherichia coli reveals a novel glycoside hydrolase family.Communications biology · 2023Article
- Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022Review
- Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose.Scientific reports · 2022Article
- β-Glucan phosphorylases in carbohydrate synthesis.Applied microbiology and biotechnology · 2021Review
- Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family.The Journal of biological chemistry · 2019Article
- Structural and thermodynamic insights into β-1,2-glucooligosaccharide capture by a solute-binding protein inThe Journal of biological chemistry · 2018Article
- Biochemical and structural analyses of a bacterialThe Journal of biological chemistry · 2017Article
- Mechanistic insight into the substrate specificity of 1,2-β-oligoglucan phosphorylase from Lachnoclostridium phytofermentans.Scientific reports · 2017Article
- Functional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocua.PloS one · 2016Article
- Crystallization and preliminary X-ray diffraction analysis of Lin1840, a putative β-glucosidase from Listeria innocua.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514.PloS one · 2014Article
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6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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