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Literature summary for 3.4.22.1 extracted from

  • Dhanavade, M.J.; Parulekar, R.S.; Kamble, S.A.; Sonawane, K.D.
    Molecular modeling approach to explore the role of cathepsin B from Hordeum vulgare in the degradation of Abeta peptides (2016), Mol. Biosyst., 12, 162-168 .
    View publication on PubMed

Application

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

Organism UniProt Comment Textmining
Hordeum vulgare F2E819
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Substrates and Products (Substrate)

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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