Investigation of Structure Function Relationships in Cathepsin B
1992; De Gruyter; Volume: 373; Issue: 2 Linguagem: Inglês
10.1515/bchm3.1992.373.2.413
ISSN0177-3593
AutoresSadiq Hasnain, C. P. Huber, Alexander Muir, Andrew D. Rowan, John S. Mort,
Tópico(s)Biochemical and Structural Characterization
ResumoPrevious suggestions from sequence alignment studies and examination of the recently determined X-ray crystal structures of cathepsin B point to roles for several specific residues in substrate binding and catalysis. The role of these groups is being examined by studying cathepsin B mutants produced using a yeast expression system. The substitutions Gly198Asp, Arg202Ala, His111Gln and Glu245Gln provide a mechanistic basis for the exopeptidase activity of cathepsin B and the ability of this cysteine proteinase to accept an arginine residue in the S2 subsite.
Referência(s)