ArticlePloS one2014
Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514.
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 11 papers.
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Who cites it
11 citing papers in PubMed.
- Dual-Activity Mannosyltransferase Phosphorylases in Family 130 of Glycoside Hydrolases.ACS catalysis · 2026Article
- Research progress and application of enzymatic synthesis of glycosyl compounds.Applied microbiology and biotechnology · 2023Review
- 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
- Analysis of the diversity of the glycoside hydrolase family 130 in mammal gut microbiomes reveals a novel mannoside-phosphorylase function.Microbial genomics · 2020Article
- Unraveling the subtleties of β-(1→3)-glucan phosphorylase specificity in the GH94, GH149, and GH161 glycoside hydrolase families.The Journal of biological chemistry · 2019Article
- Epimerization and Decomposition of Kojibiose and Sophorose by Heat Treatment under Neutral pH Conditions.Journal of applied glycoscience · 2019Article
- Identification ofThe Journal of biological chemistry · 2018Article
- Substrate adaptabilities of Thermotogae mannan binding proteins as a function of their evolutionary histories.Extremophiles : life under extreme conditions · 2016Article
- The GH130 Family of Mannoside Phosphorylases Contains Glycoside Hydrolases That Target β-1,2-Mannosidic Linkages in Candida Mannan.The Journal of biological chemistry · 2015Article
- Structural bases for N-glycan processing by mannoside phosphorylase.Acta crystallographica. Section D, Biological crystallography · 2015Article
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7 authors.
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Abstract
We characterized Teth514_1788 and Teth514_1789, belonging to glycoside hydrolase family 130, from Thermoanaerobacter sp. X-514. These two enzymes catalyzed the synthesis of 1,2-β-oligomannan using β-1,2-mannobiose and d-mannose as the optimal acceptors, respectively, in the presence of the donor α-d-mannose 1-phosphate. Kinetic analysis of the phosphorolytic reaction toward 1,2-β-oligomannan revealed that these enzymes followed a typical sequential Bi Bi mechanism. The kinetic parameters of the phosphorolysis of 1,2-β-oligomannan indicate that Teth514_1788 and Teth514_1789 prefer 1,2-β-oligomannans containing a DP ≥3 and β-1,2-Man2, respectively. These results indicate that the two enzymes are novel inverting phosphorylases that exhibit distinct chain-length specificities toward 1,2-β-oligomannan. Here, we propose 1,2-β-oligomannan:phosphate α-d-mannosyltransferase as the systematic name and 1,2-β-oligomannan phosphorylase as the short name for Teth514_1788 and β-1,2-mannobiose:phosphate α-d-mannosyltransferase as the systematic name and β-1,2-mannobiose phosphorylase as the short name for Teth514_1789.
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