Molecular cloning and characterization of Bifidobacterium bifidum 1,2-alpha-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95).

@article{Katayama2004MolecularCA,
  title={Molecular cloning and characterization of Bifidobacterium bifidum 1,2-alpha-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95).},
  author={Takane Katayama and Akiko Sakuma and Takatoshi Kimura and Yutaka Makimura and Jun Hiratake and Kanzo Sakata and Takashi Yamanoi and Hidehiko Kumagai and Kenji R. Yamamoto},
  journal={Journal of bacteriology},
  year={2004},
  volume={186 15},
  pages={4885-93}
}
A genomic library of Bifidobacterium bifidum constructed in Escherichia coli was screened for the ability to hydrolyze the alpha-(1-->2) linkage of 2'-fucosyllactose, and a gene encoding 1,2-alpha-l-fucosidase (AfcA) was isolated. The afcA gene was found to comprise 1,959 amino acid residues with a predicted molecular mass of 205 kDa and containing a signal peptide and a membrane anchor at the N and C termini, respectively. A domain responsible for fucosidase activity (the Fuc domain; amino… CONTINUE READING

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