| Activity |
|---|
| Catalytic type | Aspartic |
| Peplist | Included in the Peplist with identifier PL00003 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.23 (Aspartic endopeptidases) >> Peptidase 3.4.23.46
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (7 cleavages) |
| Activity status | human: active (Tang & Koelsch, 2004)
mouse: active (Ohno et al., 2004)
|
| Physiology | Roberds et al. (2001) concluded that this enzyme is the primary beta-secretase activity in mouse brain. |
| Knockout | A mouse gene knockout model showed that loss of beta-secretase activity led to a reduction in beta-amyloid peptide production but no profound phenotypic defects (Roberds et al., 2001). Upregulation in mouse, in the background of over-expressed Alzheimer"s precursor protein, was studied by Chiocco et al. (2004). |
| Pharmaceutical relevance | Memapsin-2 is a transmembrane aspartic endopeptidase that has beta-secretase activity, and may therefore be a drug target for Alzheimer"s disease (Ghosh et al., 2002). However, an initial report that it could be deleted in mouse without adverse effects (Roberds et al., 2001) was later denied (Laird et al., 2005), raising issues that need to be considered in relation to the potential of memapsin-2 as a therapeutic target for treatment of Alzheimer"s disease. |
| Pathways |
KEGG | Alzheimer's disease |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Memapsin_2 |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | eg/vil/-/lf d/va/-/vf (based on 25 cleavages) |
