Crystal structure of β-N-acetylglucosaminidase CbsA from Thermotoga neapolitana.

@article{Kim2015CrystalSO,
  title={Crystal structure of β-N-acetylglucosaminidase CbsA from Thermotoga neapolitana.},
  author={Jin-Sik Kim and Bo Young Yoon and Jinsook Ahn and Jaeho Cha and Nam-Chul Ha},
  journal={Biochemical and biophysical research communications},
  year={2015},
  volume={464 3},
  pages={869-74}
}
CbsA from the thermophilic marine bacteria Thermotoga neapolitana is a chitinolyitc enzyme that can cleave a glycosidic bond of the polymer N-acetylglucosamine at the non-reducing end. This enzyme has particularly high activity on di-N-acetylchitobiose. CbsA consists of a family of 3 glycoside hydrolase (GH3)-type catalytic domains and a unique C-terminal domain. The C-terminal domain distinguishes CbsA from other GH3-type enzymes. Sequence analyses have suggested that CbsA has the Asp-His dyad… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 1 time over the past 90 days. VIEW TWEETS

From This Paper

Topics from this paper.
1 Citations
0 References
Similar Papers

Citations

Publications citing this paper.

Similar Papers

Loading similar papers…