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

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 thi...