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Stem bromelain: Amino acid sequence and implications for weak binding of cystatin
Author(s) -
Ritonja Anka,
Rowan Andrew D.,
Buttle David J.,
Rawlings Neil D.,
Turk Vito,
Barrett Alan J.
Publication year - 1989
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(89)81383-3
Subject(s) - papain , bromelain , cysteine , cysteine proteinase inhibitors , biochemistry , cystatin , peptide sequence , chemistry , amino acid , enzyme , amino acid residue , sequence (biology) , biology , microbiology and biotechnology , cystatin c , gene , apoptosis , programmed cell death , renal function , caspase
The amino acid sequence of stem bromelain, the major cysteine proteinase from pineapple stem is described. It shows that the enzyme is a member of the papain superfamily of cysteine proteinases, but is not very closely related to any other known member of this group. The sequence shows mutation or deletion of several residues that have been conserved in cysteine proteinases examined previously, including Asn‐175 (papain). We suggest that some of these changes have the effect of altering the active‐site geometry of stem bromelain, and that this accounts for the resistance of the enzyme to inhibition by cystatins and E‐64 [L‐3‐carboxy‐2,3‐ trans ‐epoxypropionylleucylamido(4‐guanidino)butane].