PMID: 2489084Aug 1, 1989Paper

Hydrophobic cluster analysis of the primary sequences of alpha-amylases

International Journal of Biological Macromolecules
E RaimbaudB Henrissat

Abstract

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.

References

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Citations

Dec 1, 1992·Bio/technology·P JoyetC Gaillardin
Feb 26, 2008·Proteomics·Humberto González-DíazEugenio Uriarte
Jan 1, 1994·FEMS Microbiology Letters·A P KellyD J McConnell
Jan 1, 1997·Progress in Biophysics and Molecular Biology·S Janecek
Jun 1, 1994·International Journal of Biological Macromolecules·M BrissováM Simonetti

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