Journal of Protein Chemistry

, Volume 12, Issue 5, pp 509–514

Evolution of parallel β/α-barrel enzyme family lightened by structural data on starch-processing enzymes

  • Štefan Janeček
  • Štefan Baláž

DOI: 10.1007/BF01025115

Cite this article as:
Janeček, Š. & Baláž, Š. J Protein Chem (1993) 12: 509. doi:10.1007/BF01025115


The parallel β/α-barrel domain consisting of eight parallel β-sheets surrounded by eight α-helices has been currently identified in crystal structures of more than 20 enzymes. This type of protein folding motif makes it possible to catalyze various biochemical reactions on a variety of substrates (i.e., it seems to be robust enough so that different enzymatic functionalities could be designed on it). In spite of many efforts aimed at elucidation of evolutionary history of the present-day β/α-barrels, a challenging question remains unanswered: How has the parallel β/α-barrel fold arisen? Although the complete sequence comparison of all β/α-barrel amino acid sequences is not yet available, several sequence similarities have been revealed by using the highly conserved regions of α-amylase as structural templates. Since many starch-processing enzymes adopt the parallel β/α-barrel structure these enzymes might be useful in the search for evolutionary relationships of the whole parallel eight-folded β/α-barrel enzyme family.

Key words

β/α-Barrel enzymeα-amylaseevolutionary relationshipssequence similarities

Copyright information

© Plenum Publishing Corporation 1993

Authors and Affiliations

  • Štefan Janeček
    • 1
  • Štefan Baláž
    • 1
  1. 1.Department of Biochemical Technology, Faculty of Chemical TechnologySlovak Technical UniversityBratislavaSlovakia