Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus

J Gen Microbiol. 1989 Jun;135(6):1521-8. doi: 10.1099/00221287-135-6-1521.

Abstract

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, pullulanase and cyclodextrin glucanotransferase. All the enzymes examined contained four highly conserved regions which probably constitute the active centres of the enzymes. The amino acid residues required for the specificity of neopullulanase are compared with those of alpha-amylase and other amylolytic enzymes.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Amylases / genetics
  • Bacterial Proteins / genetics*
  • Base Sequence
  • DNA, Bacterial / genetics
  • Genes, Bacterial*
  • Geobacillus stearothermophilus / genetics*
  • Glycoside Hydrolases / genetics*
  • Molecular Sequence Data
  • Protein Conformation
  • Recombinant Proteins / genetics
  • Sequence Homology, Nucleic Acid

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Recombinant Proteins
  • Amylases
  • Glycoside Hydrolases
  • neopullulanase

Associated data

  • GENBANK/M28138