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Literature summary for 3.4.21.26 extracted from
- Purification and characterization of a prolyl endopeptidase from round scad (Decapterus maruadsi) skeletal muscle and its role in collagen degradation (2016), Mod. Food Sci. Technol., 32, 122-129 .
No PubMed abstract available
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fish muscle collagen + H2O | Decapterus maruadsi | the enzyme hydrolysis site is at the carboxyl terminus of prolyl residues | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Decapterus maruadsi | - |
round scad | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate precipitation, DEAE-Sephacel column chromatography, phenyl Sepharose column chromatography, and Q-Sepharose column chromatography | Decapterus maruadsi |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| skeletal muscle | - |
Decapterus maruadsi | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fish muscle collagen + H2O | the enzyme hydrolysis site is at the carboxyl terminus of prolyl residues | Decapterus maruadsi | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 82000, calculated from amino acid sequence | Decapterus maruadsi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PEP | - |
Decapterus maruadsi |
| prolyl endopeptidase | - |
Decapterus maruadsi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
- |
Decapterus maruadsi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Decapterus maruadsi |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 7.5 | good stability is observed in the pH range of 5.0 to 7.5 | Decapterus maruadsi |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme participates in post-mortem fish collagen degradation | Decapterus maruadsi |
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