Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Der p 1 propeptide | the propeptide of 80 amino acids plays an essential role in zymogen folding (as an intramolecular chaperone) and in the inhibition of its own enzymatic activity | Dermatophagoides pteronyssinus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-Der p 3 + H2O | Dermatophagoides pteronyssinus | activation | Der p 3 + Der p 3 propeptide | - |
? | |
pro-Der p 6 + H2O | Dermatophagoides pteronyssinus | activation | Der p 6 + Der p 6 propeptide | - |
? | |
pro-Der p 9 + H2O | Dermatophagoides pteronyssinus | activation | Der p 9 + Der p 9 propeptide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Dermatophagoides pteronyssinus | P08176 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the Der p 1 enzyme propeptide of 80 amino acids plays an essential role in zymogen folding as an intramolecular chaperone and in the inhibition of its own enzymatic activity | Dermatophagoides pteronyssinus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
midgut | immunohistochemic localisation of the enzyme | Dermatophagoides pteronyssinus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-Der p 3 + H2O | activation | Dermatophagoides pteronyssinus | Der p 3 + Der p 3 propeptide | - |
? | |
pro-Der p 3 + H2O | activation, the enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen | Dermatophagoides pteronyssinus | Der p 3 + Der p 3 propeptide | - |
? | |
pro-Der p 6 + H2O | activation | Dermatophagoides pteronyssinus | Der p 6 + Der p 6 propeptide | - |
? | |
pro-Der p 6 + H2O | pro-Der p 6 zymogen is recombinantly produced in Pichia pastoris, activation mechanism analysis by mite protease Der p 1, overview. The enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen. The N-terminal sequence of rDer p 6 is V35IGGDQ. The propeptide of proDer p 6 inhibits the proteolytic activity of protease Der p 6, but once cleaved, it is degraded by the protease | Dermatophagoides pteronyssinus | Der p 6 + Der p 6 propeptide | - |
? | |
pro-Der p 9 + H2O | activation | Dermatophagoides pteronyssinus | Der p 9 + Der p 9 propeptide | - |
? | |
pro-Der p 9 + H2O | activation, the enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen | Dermatophagoides pteronyssinus | Der p 9 + Der p 9 propeptide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Der p 1 | - |
Dermatophagoides pteronyssinus |
General Information | Comment | Organism |
---|---|---|
evolution | enzyme Der p 1 is a cysteine protease from the papain family | Dermatophagoides pteronyssinus |
additional information | activation mechanism analysis of the two other serine proteases, Der p 6 (chymotrypsin-like) and Der p 9 (collagenase)zymogen by mite protease Der p 1, overview | Dermatophagoides pteronyssinus |
physiological function | the enzyme is is the primary activator of Der p 3, Der p 6 and Der p 9 the proteolytic allergens produced by the house dust mite Dermatophagoides pteronyssinus. Der p 1 in either its recombinant formor in the natural context of house dustmite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases | Dermatophagoides pteronyssinus |