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Literature summary for 3.4.14.5 extracted from
- Purification of an X-prolyl-dipeptidyl aminopeptidase from the cell wall proteolytic system of Lactococcus lactis subsp. Cremoris (1989), Appl. Microbiol. Biotechnol., 31, 75-78.
No PubMed abstract available
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| diisopropyl fluorophosphate | - |
Lactococcus lactis |  |
| phenylmethylsulfonyl fluoride | - |
Lactococcus lactis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 90000 | - |
2 * 90000, SDS-PAGE | Lactococcus lactis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Lactococcus lactis | possible role of the enzyme seems to match the high Pro content of beta-casein | ? | - |
? | |
| additional information | Lactococcus lactis P8-2-47 | possible role of the enzyme seems to match the high Pro content of beta-casein | ? | - |
? | |
| additional information | Lactococcus lactis subsp. cremoris | possible role of the enzyme seems to match the high Pro content of beta-casein | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactococcus lactis | - |
subsp. cremonis, P8-2-47 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Lactococcus lactis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 90 | - |
- |
Lactococcus lactis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Ala-Pro-4-nitroanilide + H2O | - |
Lactococcus lactis | Ala-Pro + 4-nitroaniline | - |
? | |
| Ala-Pro-4-nitroanilide + H2O | - |
Lactococcus lactis P8-2-47 | Ala-Pro + 4-nitroaniline | - |
? | |
| Ala-Pro-4-nitroanilide + H2O | - |
Lactococcus lactis subsp. cremoris | Ala-Pro + 4-nitroaniline | - |
? | |
| beta-casein + H2O | cleavage of the proline-rich sequence | Lactococcus lactis | ? | - |
? | |
| beta-casein + H2O | cleavage of the proline-rich sequence | Lactococcus lactis P8-2-47 | ? | - |
? | |
| beta-casein + H2O | cleavage of the proline-rich sequence | Lactococcus lactis subsp. cremoris | ? | - |
? | |
| Gly-Pro-4-nitroanilide + H2O | - |
Lactococcus lactis | Gly-Pro + 4-nitroaniline | - |
? | |
| Gly-Pro-4-nitroanilide + H2O | - |
Lactococcus lactis P8-2-47 | Gly-Pro + 4-nitroaniline | - |
? | |
| Gly-Pro-4-nitroanilide + H2O | - |
Lactococcus lactis subsp. cremoris | Gly-Pro + 4-nitroaniline | - |
? | |
| additional information | possible role of the enzyme seems to match the high Pro content of beta-casein | Lactococcus lactis | ? | - |
? | |
| additional information | possible role of the enzyme seems to match the high Pro content of beta-casein | Lactococcus lactis P8-2-47 | ? | - |
? | |
| additional information | possible role of the enzyme seems to match the high Pro content of beta-casein | Lactococcus lactis subsp. cremoris | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 90000, SDS-PAGE | Lactococcus lactis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | 50 | - |
Lactococcus lactis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
rapid inactivation above | Lactococcus lactis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Lactococcus lactis |
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