| Activity |
|---|
| Catalytic type | Metallo |
| Peplist | Included in the Peplist with identifier PL00125 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.11 (Aminopeptidases) >> Peptidase 3.4.11.7
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (3 cleavages) |
| Activity status | human: active (Wang & Cooper, 2004)
mouse: active (Vazeux et al., 1997)
|
| Physiology | Ectoenzyme degrading angiotensin II. |
| Knockout | Mice homozygous for deficiency of the enzyme developed normally, generated normal numbers of T and B cells, exhibited normal antibody responses to both thymus-dependent and -independent antigens, and showed normal serum immunoglobulin levels. It was therefore concluded that the enzyme is not essential for normal B and T cell development (Lin et al., 1998). However, although the deficient mice developed normally, they failed to mount the expected angiogenic response to hypoxia or growth factors (Marchio et al., 2004). |
| Pharmaceutical relevance | Aminopeptidase A is involved in the formation of brain angiotensin III, which exerts a tonic stimulatory action on the central control of blood pressure. Thus, central inhibitors of aminopeptidase A constitute putative central antihypertensive agents (Rozenfeld et al., 2002; Fournie-Zaluski et al., 2004). The enzyme also is a regulator of blood vessel formation, and is a putative target for angiogenesis in cancer. |
| Pathways |
KEGG | Renin-angiotensin system |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Glutamyl_aminopeptidase |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | -/-/-/Ed e/-/-/- (based on 14 cleavages) |
