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

• Published in: Biochimica et biophysica acta. General subjects Vol. 1861; no. 12; pp. 3231 - 3237
• Main Authors: Awad, Faisal Nureldin, Laborda, Pedro, Wang, Meng, Lu, Ai Min, Li, Qian, Cai, Zhi Peng, Liu, Li, Voglmeir, Josef
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2017
• Subjects: bacteria; Carbohydrate active enzyme; Catalysis; Enzymatic synthesis; Flavobacteriaceae - enzymology; Glycoside hydrolase family 130; glycosides; mannose; Mannose - metabolism; Mannosides - biosynthesis; matrix-assisted laser desorption-ionization mass spectrometry; nuclear magnetic resonance spectroscopy; Phosphorolysis; phosphorylase; Phosphorylases - chemistry; Phosphorylases - isolation & purification; Phosphorylases - metabolism; Recombinant Proteins - biosynthesis; Recombinant Proteins - isolation & purification; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Substrate Specificity; Zobellia; Zobellia galactanivorans; β-Mannan; β-Mannoside; Enzymatic synthesis; Phosphorolysis; Zobellia galactanivorans; β-Mannan; β-Mannoside; Glycoside hydrolase family 130; Carbohydrate active enzyme
• ISSN: 0304-4165; 1872-8006
• DOI: 10.1016/j.bbagen.2017.09.013

Mannoside 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. The 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. We 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). An unique bacterial phosphorylase specifically targeting β-1,3-mannoside linkages was discovered. Functional extension of glycoside hydrolase family 130. [Display omitted] •Mannoside phosphorylases are frequently found in bacteria and play an important role in carbohydrate processing.•A bacterial phosphorylase catalyzes the reversible phosphorolysis of novel β-1,3-oligomannose structures.•Discovery of an enzyme specifically targets β-1,3-mannoside linkages.•Functional extension of glycoside hydrolase family 130