RRC ID 40753
Author Shimada Y, Watanabe Y, Wakinaka T, Funeno Y, Kubota M, Chaiwangsri T, Kurihara S, Yamamoto K, Katayama T, Ashida H.
Title α-N-Acetylglucosaminidase from Bifidobacterium bifidum specifically hydrolyzes α-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin.
Journal Appl Microbiol Biotechnol
Abstract α-Linked N-acetylglucosamine is one of the major glyco-epitopes in O-glycan of gastroduodenal mucin. Here, we identified glycoside hydrolase (GH) family 89 α-N-acetylglucosaminidase, termed AgnB, from Bifidobacterium bifidum JCM 1254, which is essentially specific to GlcNAcα1-4Gal structure. AgnB is a membrane-anchored extracellular enzyme consisting of a GH89 domain and four carbohydrate-binding module (CBM) 32 domains. Among four CBM32 domains, three tandem ones at C-terminus showed to bind porcine gastric mucin, suggesting that these domains enhance the enzyme activity by increasing affinity for multivalent substrates. AgnB might be important for assimilation of gastroduodenal mucin by B. bifidum and also applicable to production of prebiotic oligosaccharides from porcine gastric mucin.
Volume 99(9)
Pages 3941-8
Published 2015-5-1
DOI 10.1007/s00253-014-6201-x
PMID 25381911
MeSH Acetylglucosamine / metabolism* Acetylglucosaminidase / metabolism* Bifidobacterium / enzymology* Binding Sites Gastric Mucins / metabolism*
IF 3.53
Times Cited 11
General Microbes JCM 1254 JCM 1275 JCM 7046 JCM 7096 JCM 10602 JCM 1255 JCM 7004 JCM 1192 JCM 1194 JCM 1195 JCM 8224 JCM 1217 JCM 7054 JCM 1210 JCM 1222 JCM 1200 JCM 1205 JCM 12489