Prospecting for Microbial Α-N-acetylgalactosaminidases Yields a New Class of GH31 O-glycanase
Journal of biological chemistry/The Journal of biological chemistry(2019)
摘要
α-Linked GalNAc (α-GalNAc) is most notably found at the nonreducing terminus of the blood type–determining A-antigen and as the initial point of attachment to the peptide backbone in mucin-type O-glycans. However, despite their ubiquity in saccharolytic microbe-rich environments such as the human gut, relatively few α-N-acetylgalactosaminidases are known. Here, to discover and characterize novel microbial enzymes that hydrolyze α-GalNAc, we screened small-insert libraries containing metagenomic DNA from the human gut microbiome. Using a simple fluorogenic glycoside substrate, we identified and characterized a glycoside hydrolase 109 (GH109) that is active on blood type A-antigen, along with a new subfamily of glycoside hydrolase 31 (GH31) that specifically cleaves the initial α-GalNAc from mucin-type O-glycans. This represents a new activity in this GH family and a potentially useful new enzyme class for analysis or modification of O-glycans on protein or cell surfaces.
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关键词
glycosidase,glycobiology,metagenomics,glycoprotein,blood,glycopeptide cleavage,glycoside hydrolase 31 (GH31),human gut microbiome,mucin,O-glycoprotein,metagenomic analysis,glycoside hydrolase 109 (GH109),O-glycanase,N-acetylgalactosamine (alpha-GalNAc)
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