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Literature summary for 3.4.22.6 extracted from
- Structural characterization of the papaya cysteine proteinases at low pH (2006), Biochem. Biophys. Res. Commun., 341, 620-626.
Application
| Application | Comment | Organism |
|---|---|---|
| nutrition | at low pH, enzyme undergoes conformational transition leading to instability and rapid degradation by pepsin. To be effective in gut after oral administration, enzyme needs to be protected against acid denaturation and degradation | Carica papaya |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Carica papaya | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| latex | - |
Carica papaya | - |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 1 | - |
at low pH, the enzyme undergoes a conformational transition that instantaneously converts their native form into molten globule that are quite unstable and rapidly degraded by pepsin. The denatured state of these proteinase which results from acid treatment is completely irreversible | Carica papaya |
| 2 | 3 | enzyme undergoes conformational transition that instantaneously converts the native form into a molten globule state and is completely irreversible | Carica papaya |
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Release 2023.1 (January 2023)
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