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Protein Engineering vol. 8 no. 8 pp. 809-813, 1995
© 1995 Oxford University Press

RESEARCH-ARTICLE

Functionally essential, invariant glutamate near the C-terminus of strand ß5 in various ({alpha}/ß)8-barrel enzymes as a possible indicator of their evolutionary relatedness

Stefan Janecek1 and Stefan Baláz2

Institute of Ecobiology, Slovak Academy of Sciences Stefánikova 3, SK-81434 Bratislava, Slovakia 2Department of Biochemical Technology, Faculty of Chemical Technology, Slovak Technical University RadlinskSho 9, SK-81237 Bratislava, Slovakia

1To whom correspondence should be addressed

Twelve different ({alpha}/ß)8-barrel enzymes belonging to three structurally distinct families were found to contain, near the C-terminus of their strand ß5, a conserved invariant glutamic acid residue that plays an important functional role in each of these enzymes. The search was based on the idea that a conserved sequence region of an ({alpha}/ß)8-barrel enzyme should be more or less conserved also in the equivalent part of the structure of the other enzymes with this folding motif owing to their mutual evolutionary relatedness. For this purpose, the sequence region around the well conserved fifth ß-strand of a-amylase containing catalytic glutamate (Glu230, Aspergillus oryzae {alpha}-amylase numbering), was used as the sequence-structural template. The isolated sequence stretches of the 12 ({alpha}/ß)8-barrels are discussed from both the sequence-structural and the evolutionary point of view, the invariant glutamate residue being proposed to be a joining feature of the studied group of enzymes remaining from their ancestral ({alpha}/ß)8-barrel

Keywords: ({alpha}/ß)8-barrel enzyme/conserved glutamate/evolutionary/relationships/fifth ß-strand

Received March 16, 1995; revised May 10, 1995; accepted May 25, 1995.


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