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Amino acid sequence of human liver cathepsin B
Author(s) -
Ritonja Anka,
Popovic Tatjana,
Turk Vito,
Wiedenmann Karin,
Machleidt Werner
Publication year - 1985
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(85)81136-4
Subject(s) - cyanogen bromide , edman degradation , cathepsin o , cathepsin e , biochemistry , peptide sequence , cathepsin h , cathepsin a , cathepsin b , proteolysis , cathepsin , enzyme , chemistry , amino acid , papain , cleavage (geology) , cysteine , cathepsin d , cathepsin l1 , biology , gene , paleontology , fracture (geology)
The complete amino acid sequence of cathepsin B (EC 3.4.22.1) from human liver was determined. The 252‐residue sequence was obtained by automated solid‐phase Edman degradation of the light and heavy chain resulting from limited proteolysis of the single‐chain enzyme and of fragments produced by cyanogen bromide and enzymatic cleavage of the heavy chain. Human liver cathepsin B has 83.7% identical residues with the corresponding enzyme from rat liver. Comparison of both mammalian cathepsin B sequences with the sequence of papain provides further evidence that lysosomal and plant cysteine proteinases have evolved from a common ancestor and share a similar catalytic mechanism.