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Literature summary for 3.4.21.36 extracted from
- Role of protein-solvent interactions in refolding. Effects of cosolvent additives on the renaturation of porcine pancreatic elastase at various pHs (2000), Arch. Biochem. Biophys., 375, 220-228.
General Stability
| General Stability | Organism |
|---|---|
| when the native structure is achieved, cosolvents increase the stability of the enzyme to the same extent as does the acylation of the active center residue Ser195. Dimethylsulfoxide, glycerol and methanol enhance the stability of the intermediates able to refold into the native form, contrary to acetonitrile | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| renatured by dilution in the solution of substrate at various pHs under agitation. A lag period is observed before reaching the steady state of the hydrolysis of an amide substrate, and the lag period measured with the refolding enzyme is longer than that measured with the native elastase | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| pancreas | - |
Sus scrofa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinyl-Ala-Ala-Ala-4-nitroanilide + H2O | - |
Sus scrofa | succinyl-Ala-Ala-Ala + 4-nitroaniline | - |
? |  |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Sus scrofa |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | 10.5 | pH 6.8: about 45% of maximal activity, pH 10.5: about 45% of maximal activity, succinyl-Ala-Ala-Ala-4-nitroanilide | Sus scrofa |
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Release 2023.1 (January 2023)
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