Prospecting for microbial α-N-acetylgalactosaminidases yields a new class of GH31 O-glycanase.
J Biol Chem
; 294(44): 16400-16415, 2019 11 01.
Article
em En
| MEDLINE
| ID: mdl-31530641
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Alfa-N-Acetilgalactosaminidase
/
Glicosídeo Hidrolases
Limite:
Humans
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Canadá