Characterization of the Cytosolic β-N-Acetylglucosaminidase from Bifidobacterium longum subsp. longum

DOI Web Site Web Site 被引用文献5件 参考文献31件
  • Honda Yuji
    National Food Research Institute, National Agriculture and Food Research Organization Department of Food Science, Ishikawa Prefectural University
  • Nishimoto Mamoru
    National Food Research Institute, National Agriculture and Food Research Organization
  • Katayama Takane
    Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University
  • Kitaoka Motomitsu
    National Food Research Institute, National Agriculture and Food Research Organization

書誌事項

タイトル別名
  • Characterization of the Cytosolic β-<i>N</i>-Acetylglucosaminidase from <i>Bifidobacterium longum</i> subsp. <i>longum</i>

この論文をさがす

抄録

The BLLJ_1391 protein from Bifidobacterium longum subsp. longum JCM1217, a cytosolic β-N-acetylglucosaminidase belonging to glycoside hydrolase family (GH) 20, hydrolyzed lacto-N-triose II (LNTri) as well as chitin oligosaccharides. Its reaction was found to follow a substrate-assisted mechanism with anomeric retention, which is common for GH 20 enzymes. Homologous enzymes are found in genomic sequences of B. longum subsp. infantis, Bifidobacterium bifidum, and Bifidobacteium breve, all of which are infant gut-associated species of Bifidobacterium. The distribution resembles that of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase, suggesting that the enzyme plays a role in metabolism of human milk oligosaccharides by hydrolyzing LNTri generated via the cytosolic hydrolysis of lacto-N-tetraose (LNT) by LNT 1,3-β-galactosidase.

収録刊行物

被引用文献 (5)*注記

もっと見る

参考文献 (31)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ