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Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptideMajerle, Andreja ; Jerala, RomanThe proregion fits tightly into the active site in the tertiary structure of procathepsin L and prevents its activity. We show that complexes between enzyme precursor and its endogenous protein ... inhibitors--the cystatins--can be formed without prior proteolytic removal of the propeptide. Complexes between cystatins and procathepsin L are formed at acidic pH and their formation is facilitated by acidic oligosaccharides. Binding of the inhibitor to the proenzyme is reversible and the slow dissociation of complex around neutral pH may serve as a pool for the sustained release of the enzyme. Formation of the complex between cystatin and procathepsin L increases the susceptibility of the proregion to proteolytic cleavage. This process may constitute an alternative mechanism of formation of the complex between enzyme and inhibitor without prior activation of the proenzyme.Source: Archives of biochemistry and biophysics. - ISSN 0003-9861 (Vol. 417, no. 1, 2003, str. 53-58)Type of material - article, component partPublish date - 2003Language - englishCOBISS.SI-ID - 2872090
Author
Majerle, Andreja |
Jerala, Roman
Topics
biotechnology |
cystein protease procursor |
cystatin |
complex |
propeptide |
activation
source: Archives of biochemistry and biophysics. - ISSN 0003-9861 (Vol. 417, no. 1, 2003, str. 53-58)
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Database name | Field | Year |
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Majerle, Andreja | 17917 |
Jerala, Roman | 06628 |
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