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Poliovirus‐encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families
Author(s) -
Gorbalenya A.E.,
Blinov V.M.,
Donchenko A.P.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80095-3
Subject(s) - serine , proteases , cysteine , cathepsin , biochemistry , cathepsin a , biology , trypsin , serine proteinase inhibitors , proteinase 3 , deubiquitinating enzyme , cathepsin l , protease , serine protease , peptide sequence , enzyme , amino acid , cathepsin b , cysteine protease , genetics , gene , antibody , ubiquitin , autoantibody
Here we demonstrate significant similarities between the amino acid sequences of trypsin (a serine protease) and the N‐terminal piece of a specific fragment of the poliovirus polyprotein encompassing the sequence of the viral proteinase 3C, and also between cathepsin H (a cysteine protease) and the C‐terminal piece of the same fragment. A coherent alignment of the sequences of the 3 proteases was obtained, in which the principal catalytically active residues occupy identical positions. A hypothesis is proposed that the viral enzyme may provide an evolutionary link between serine and cysteine protease families.