Journal of Molecular Evolution

, Volume 45, Issue 3, pp 322–331

Domain Evolution in the α-Amylase Family

  • Stefan  Janecek
  • Birte  Svensson
  • Bernard  Henrissat

DOI: 10.1007/PL00006236

Cite this article as:
Janecek, S., Svensson, B. & Henrissat, B. J Mol Evol (1997) 45: 322. doi:10.1007/PL00006236

Abstract.

The available amino acid sequences of the α-amylase family (glycosyl hydrolase family 13) were searched to identify their domain B, a distinct domain that protrudes from the regular catalytic (β/α)8-barrel between the strand β3 and the helix α3. The isolated domain B sequences were inspected visually and also analyzed by Hydrophobic Cluster Analysis (HCA) to find common features. Sequence analyses and inspection of the few available three-dimensional structures suggest that the secondary structure of domain B varies with the enzyme specificity. Domain B in these different forms, however, may still have evolved from a common ancestor. The largest number of different specificities was found in the group with structural similarity to domain B from Bacillus cereus oligo-1,6-glucosidase that contains an α-helix succeeded by a three-stranded antiparallel β-sheet. These enzymes are α-glucosidase, cyclomaltodextrinase, dextran glucosidase, trehalose-6-phosphate hydrolase, neopullulanase, and a few α-amylases. Domain B of this type was observed also in some mammalian proteins involved in the transport of amino acids. These proteins show remarkable similarity with (β/α)8-barrel elements throughout the entire sequence of enzymes from the oligo-1,6-glucosidase group. The transport proteins, in turn, resemble the animal 4F2 heavy-chain cell surface antigens, for which the sequences either lack domain B or contain only parts thereof. The similarities are compiled to indicate a possible route of domain evolution in the α-amylase family.

Key words:α-Amylase family — Glycosyl hydrolase family 13 — Hydrophobic Cluster Analysis — (β/α)8-Barrel — Domain B — Amino acid transport-related proteins — 4F2 Heavy-chain cell surface antigens — Evolutionary relatedness 

Copyright information

© Springer-Verlag New York Inc. 1997

Authors and Affiliations

  • Stefan  Janecek
    • 1
  • Birte  Svensson
    • 2
  • Bernard  Henrissat
    • 3
  1. 1.Institute of Microbiology, Slovak Academy of Sciences, Stefánikova 3, SK-81434 Bratislava, SlovakiaCS
  2. 2.Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Copenhagen Valby, DenmarkDK
  3. 3.Centre de Recherches sur les Macromolécules Végétales, C.N.R.S., BP 53, F-38041 Grenoble Cédex, FranceFR

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