Title : S2' substrate specificity and the role of His110 and His111 in the exopeptidase activity of human cathepsin B.

Pub. Date : 2002 Feb 1

PMID : 11802791






2 Functional Relationships(s)
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1 The ability of the lysosomal cysteine protease cathepsin B to function as a peptidyldipeptidase (removing C-terminal dipeptides) has been attributed to the presence of two histidine residues (His(110) and His(111)) present in the occluding loop, an extra peptide segment located in the primed side of the active-site cleft. Dipeptides cathepsin B Homo sapiens
2 These studies showed that cathepsin B is optimized to act as an exopeptidase, cleaving dipeptides from protein substrates in a successive manner, because of its relaxed specificity in P2" and its other subsites. Dipeptides cathepsin B Homo sapiens