Abstract:
:Stopped-flow kinetics showed that the inhibition of the lysosomal cysteine proteinase, cathepsin B, by its endogenous inhibitor, cystatin C, occurs by a two-step mechanism, in which an initial, weak interaction is followed by a conformational change. The initial interaction most likely involves binding of the N-terminal region of the inhibitor to the proteinase. Considerable evidence indicates that the subsequent conformational change is due to the inhibitor displacing the occluding loop of the proteinase that partially obscures the active site. The presence of this loop, which allows the enzyme to function as an exopeptidase, thus complicates the inhibition mechanism, rendering cathepsin B much less susceptible than other cysteine proteinases to inhibition by cystatins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nycander M,Estrada S,Mort JS,Abrahamson M,Björk Idoi
10.1016/s0014-5793(97)01604-9subject
Has Abstractpub_date
1998-01-23 00:00:00pages
61-4issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(97)01604-9journal_volume
422pub_type
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