Discovery and biochemical characterization of a mannose Phosphorylase catalyzing the synthesis of novel β-1,3-Mannosides

Publication date: Available online 19 September 2017
Source:Biochimica et Biophysica Acta (BBA) - General Subjects
Author(s): Faisal Nureldin Awad, Pedro Laborda, Meng Wang, Ai Min Lu, Qian Li, Zhi Peng Cai, Li Liu, Josef Voglmeir
BackgroundMannoside phosphorylases are frequently found in bacteria and play an important role in carbohydrate processing. These enzymes catalyze the reversible conversion of β-1,2- or β-1,4-mannosides to mannose and mannose-1-phosphate in the presence of inorganic phosphate.MethodsThe biochemical parameters of this recombinantly expressed novel mannose phosphorylase were obtained. Furthermore purified reaction products were subjected to ESI- and MALDI-TOF mass spectrometry and detailed NMR analysis to verify this novel type of β-1,3-mannose linkage.ResultsWe describe the first example of a phosphorylase specifically targeting β-1,3-mannoside linkages. In addition to mannose, this phosphorylase originating from the bacterium Zobellia galactanivorans could add β-1,3-linked mannose to various other monosaccharides and anomerically modified 5-bromo-4-chloro-3-indolyl-glycosides (X-sugars).ConclusionsAn unique bacterial phosphorylase specifically targeting β-1,3-mannoside linkages was discovered.General Significance.Functional extension of glycoside hydrolase family 130.

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