| Activity |
|---|
| Catalytic type | Metallo |
| Peplist | Included in the Peplist with identifier PL00228 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.13 (Dipeptidases) >> Peptidase 3.4.13.19
|
| Enzymology | BRENDA database |
| Activity | Membrane dipeptidase hydrolyses a wide variety of dipeptides regardless of whether the C-terminal residue is in the D or L configuration (<%Hooper, 2004[20040525A436]%>). An that was discovered very early in the study of the enzyme is the hydrolysis of dehydro-dipeptides suchas Gly-dehydroPhe, and the enzyme has been known as dehydrodipeptidase I (<%Campbell, 1970[20040511P974]%>). Activity is not confined to peptides: membrane dipeptidase is the only mammalian beta-lactamase (<%Campbell %etal, 1984[20040831A936]%>) and has also attracted interest for the conversion of leukotriene-D4 to leukotriene-E4 (<%An %etal, 1994[20040510W954]%>). |
| Activity status | human: active (Hooper, 2004)
mouse: active (Satoh et al., 1993)
|
| Inhibitors | Membrane dipeptidase is inhibited by cilastatin (IC50 0.1 mM), and this compound has been used therapeutically to retard the destruction of beta-lactam antibiotics (Kahan et al., 1983). More potent, aminophosphinic acid inhibitors have also been described (Gurulingappa et al., 2004). |
| Physiology | Extracellular catabolism of glutathione. Inactivates leukotriene D4 in the lung. The only mammalian beta-lactamase. Also suggested to maintain oxidising conditions in endoplasmic reticulum |
| Knockout | Gene deletion in mice had no effect on viability or fertility. The mutant mice retain partial ability to convert leukotriene D4 to leukotriene E4 (Habib et al., 1998). |
| Pharmaceutical relevance | Destroys thienamycin and imipenem in the kidney, and to prevent this, the inhibitor cilastatin is co-administered with the antibiotics. |
|
Other databases
| TREEFAM | http://www.treefam.org/family/TF324523 |
