Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus.

@article{Kuriki1989NucleotideSO,
  title={Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus.},
  author={Takashi Kuriki and Tadayuki Imanaka},
  journal={Journal of general microbiology},
  year={1989},
  volume={135 6},
  pages={
          1521-8
        }
}
The gene (nplT) for a new type of pullulan-hydrolysing enzyme, neopullulanase, from Bacillus stearothermophilus TRS40 was sequenced. The DNA sequence revealed only one large open reading frame, composed of 1764 bases and 588 amino acid residues (Mr 69144). Although the thermostable neopullulanase contained eight cysteine residues, they did not provide conformational stability by disulphide bonds. A comparison was made of the amino acid sequences of alpha-amylase, neopullulanase, isoamylase… CONTINUE READING

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