The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity.

@article{Leemhuis2003TheFC,
  title={The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity.},
  author={Hans Leemhuis and Henri{\"e}tte J. Rozeboom and Bauke W Dijkstra and Lubbert Breitling Dijkhuizen},
  journal={FEBS letters},
  year={2003},
  volume={541 1-3},
  pages={47-51}
}
The alpha-amylase family is a large group of starch processing enzymes [Svensson, B. (1994) Plant Mol. Biol. 25, 141-157]. It is characterized by four short sequence motifs that contain the seven fully conserved amino acid residues in this family: two catalytic carboxylic acid residues and four substrate binding residues. The seventh conserved residue (Asp135) has no direct interactions with either substrates or products, but it is hydrogen-bonded to Arg227, which does bind the substrate in the… CONTINUE READING