Article
S2' substrate specificity and the role of His110 and His111 in the exopeptidase activity of human cathepsin B.
The Biochemical journal - 1 Feb 2002
Krupa Joanne C, Hasnain Sadiq, Nägler Dorit K, Ménard Robert, Mort John S
Abstract excerpt
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. Whereas His(111) is unpaired, His(110) is present as an ion pair with Asp(22) on the main...
Topics
- Amidohydrolases
- Aspartic Acid
- Binding Sites
- Cathepsin B
- Exopeptidases
- Glutamic Acid
- Histidine
- Humans
- Ions
- Kinetics
- Lysosomes
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Binding