Deduced amino acid sequence and possible catalytic residues of a thermostable, alkaline cellulase from an Alkaliphilic bacillus strain.

@article{Hakamada2000DeducedAA,
  title={Deduced amino acid sequence and possible catalytic residues of a thermostable, alkaline cellulase from an Alkaliphilic bacillus strain.},
  author={Yoshihiro Hakamada and Yuji Hatada and Kenzo Koike and Tadashi Yoshimatsu and Shuji Kawai and Tetsuo Kobayashi and Susumu Ito},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2000},
  volume={64 11},
  pages={2281-9}
}
Alkaliphilic Bacillus sp. strain KSM-S237 (a relative of Bacillus pseudofirmus) produces a thermostable, alkaline endo-1,4-beta-glucanase (Egl). The entire gene for the enzyme harbored a 2,472-bp open reading frame (ORF) encoding 824 amino acids, including a 30-aminoacid signal peptide. The deduced amino acid sequence of the mature enzyme (794 amino acids, 88,284 Da) showed very high similarity to those of family 5 mesophilic, alkaline Egls from some alkaliphilic bacilli. The enzyme had a… CONTINUE READING
13 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 13 extracted citations

Similar Papers

Loading similar papers…