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Literature summary for 3.4.23.22 extracted from
- Endothiapepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 104-107.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| nutrition | the enzyme can be used as a fungal rennet in cheese production | Cryphonectria parasitica |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis | Cryphonectria parasitica |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| using ammonium sulfate as precipitant at pH 4.6, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiple isomorphous replacement | Cryphonectria parasitica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| L363564 | statine-containing renin inhibitor, hydrogen bonding interaction witht the enzyme, e.g. via Asp32 and Asp215, overview | Cryphonectria parasitica |  |
| pepstatin A | strong inhibition, the inhibitor motif -CH(OH)-CH2- mimicks the tetrahedral intermdiate of the catalytic reaction | Cryphonectria parasitica | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 33800 | - |
x * 33800 | Cryphonectria parasitica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cryphonectria parasitica | - |
i.e. Cryphonectria parasitica, the chestnut blight fungus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O | i.e. oxidized insulin B chain, cleavage site specificity | Cryphonectria parasitica | FVN + Gln + HLCGSHL + VEALY + LVCGERGF + FYTPKA | - |
? | |
| kappa-casein + H2O | reaction contributes to milk-clotting activity, cleavage site specificity for Ser104-Phe105 | Cryphonectria parasitica | ? | - |
? | |
| additional information | the enzyme prefers protein substrates with hydrophobic amino acid residues at P1 and P1' positions | Cryphonectria parasitica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 33800 | Cryphonectria parasitica |
| More | structure analysis, overview | Cryphonectria parasitica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
acidic pH optimum | Cryphonectria parasitica |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Cryphonectria parasitica | about | - |
5.5 |
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Release 2023.1 (January 2023)
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