Application | Comment | Organism |
---|---|---|
medicine | three dimensional structure of cathepsin B from Hordeum vulgare is predicted by using a homology modeling technique. The sequence and structure analysis reveal that the active site residues of cathepsin B from Hordeum vulgare are exactly the same to human cathepsin B. Probable involvement in the cleavage of amyloid beta peptide. Hence, the structure of cathepsin B from Hordeum vulgare can be useful to study Abeta peptide degradation in detail at the atomic level. Thus, this study might be useful to understand amyloid beta peptide degradation as well as to design alternative strategies to control Alzheimer's disease | Hordeum vulgare |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hordeum vulgare | F2E819 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Abeta peptide + H2O | the enzyme cleaves the Abeta peptide from the carboxylic end of Glu11 | Hordeum vulgare | ? | - |
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