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Literature summary for 3.4.23.29 extracted from
- Polyporopepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 113-115.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis | Irpex lacteus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallization by hanging drop method with ammonium sulfate as precipitant, X-ray diffraction structure determination and analysis at 1.9 A resolution | Irpex lacteus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1,2-epoxy-3-(4-nitrophenoxy)propane | inactivation, active site-directed inhibitor | Irpex lacteus |  |
| Diazoacetyl-DL-norleucine methyl ester | inactivation, active site-directed inhibitor | Irpex lacteus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 36000 | - |
x * 36000, SDS-PAGE | Irpex lacteus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Irpex lacteus | - |
formerly Irpex lacteus | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | two possible N-glycosylation sites at Asn192 and Asn228, the enzyme shows affinity for concanavalin A, wheat germ agglutinin, and Ricinus communis agglutinin | Irpex lacteus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme by dehydroacetylpepstatin affinity chromatography | Irpex lacteus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha1-casein + H2O | cleavage of Phe23-Phe24 and Lys103-Tyr104 bonds at pH 6.0 | Irpex lacteus | ? | - |
? | |
| beta-casein + H2O | cleavage of Leu165-Ser166, Ala189-Phe190, and Leu192-Tyr193 bonds, no cleavage of Leu139-Leu140 and Ser142-Trp143 bonds | Irpex lacteus | ? | - |
? | |
| FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O | i.e. insulin B chain, cleavage site specificity at pH 3.0.the Ala14-Leu15 bond is preferred | Irpex lacteus | FVNQHLCGSHL + VEA + LYLVCGERGF + FYT + PKA | - |
? | |
| Hemoglobin + H2O | - |
Irpex lacteus | ? | - |
? | |
| kappa-casein + H2O | cleavage of Phe105-Met106 bond | Irpex lacteus | ? | - |
? | |
| additional information | the enzyme requires hydrophobic amino acids at P3 and/or P4 positions, the enzyme shows high milk-clotting activity, no activity with trypsinogen, pig pepsin, and mucorpepsins | Irpex lacteus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 36000, SDS-PAGE | Irpex lacteus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| milk-clotting enzyme | - |
Irpex lacteus |
| More | the enzyme belongs to the A1 peptidase family | Irpex lacteus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme is the least heat-stable among the milk-clotting enzymes | Irpex lacteus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 2.8 | 2.9 | substrates casein and hemoglobin | Irpex lacteus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Irpex lacteus | - |
- |
5.3 |
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