English Journal

Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease.

Niemer M1, Mehofer U1, Verdianz M1, Porodko A1, Schähs P1, Kracher D2, Lenarcic B3, Novinec M3, Mach L4.
Biochimie.Biochimie.2016 Mar;122:119-25. doi: 10.1016/j.biochi.2015.06.017. Epub 2015 Jul 9.
The tobacco-related plant species Nicotiana benthamiana has recently emerged as a versatile expression platform for the rapid generation of recombinant biopharmaceuticals, but product yield and quality frequently suffer from unintended proteolysis. Previous studies have highlighted that recombinant
PMID 26166069

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

Krupa JC1, Hasnain S, Nägler DK, Ménard R, Mort JS.
The Biochemical journal.Biochem J.2002 Feb 1;361(Pt 3):613-9.
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
PMID 11802791

Illy C1, Quraishi O, Wang J, Purisima E, Vernet T, Mort JS.
The Journal of biological chemistry.J Biol Chem.1997 Jan 10;272(2):1197-202.
Within the lysosomal cysteine protease family, cathepsin B is unique due to its ability to act both as an endopeptidase and a peptidyldipeptidase. This latter capacity to remove C-terminal dipeptides has been attributed to the presence of a 20-residue insertion, termed the occluding loop, that block
PMID 8995421