Investigation of structure function relationships in cathepsin B.
Previous 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.
Hasnain
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S
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
Huber
C P
CP
Muir
A
A
Rowan
A D
AD
Mort
J S
JS
D000595:Amino Acid Sequence; D000818:Animals; D002401:Cathepsin B / Q000032:analysis*; D005998:Glycine / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D010206:Papain / Q000032:analysis; D051381:Rats; D014961:X-Ray Diffraction; D015003:Yeasts / Q000201:enzymology
D002401:Cathepsin B; D010206:Papain; D005998:Glycine