| 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
|
|
WOS Category
|
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
|
| Resource |
| 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 |
