Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10756103 | Biochemical and Biophysical Research Communications | 2014 | 6 Pages |
Abstract
- The structures of active cathepsin A and the inactive precursor are very similar.
- The only major difference is the absence of a 40 residue activation domain.
- The termini of the active catalytic core are held together by a disulfide bond.
- Compound 1 reacts with the catalytic Ser150, building a tetrahedral intermediate.
- Compound 2 is cleaved by the enzyme and a fragment remained bound.
Keywords
Related Topics
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Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Herman A. Schreuder, Alexander Liesum, Katja Kroll, Britta Böhnisch, Christian Buning, Sven Ruf, Thorsten Sadowski,