Hydrophobic cluster analysis of the primary sequences of alpha-amylases.
The amino acid sequences of 18 alpha-amylases have been compared by hydrophobic cluster analysis. The method was first calibrated with two alpha-amylases (Aspergillus oryzae and pig pancreas) whose three-dimensional structures are known. It was then applied to the other alpha-amylases resulting in straightforward sequence alignments which could be used for structure prediction. It was found that all alpha-amylases which were investigated display the same basic super-secondary structure with a (beta alpha)8 barrel. Most of the secondary structure elements of the protein cores could be assigned to segments of the amino acid sequences. In addition, six sub-families could be identified, based upon specific similarities occurring in the variable regions of alpha-amylases.
Raimbaud
E
E
Institut National de la Recherche Agronomique, Nantes, France.
Buleon
A
A
Perez
S
S
Henrissat
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001236:Aspergillus oryzae; D001407:Bacillus; D001467:Hordeum; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D013302:Streptomyces; D013552:Swine; D000516:alpha-Amylases / Q000737:chemistry*
D000516:alpha-Amylases