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Literature summary extracted from

  • Jaspard, E.
    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.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.21.36 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

EC Number Organism UniProt Comment Textmining
3.4.21.36 Sus scrofa
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.4.21.36 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

EC Number Source Tissue Comment Organism Textmining
3.4.21.36 pancreas
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.36 succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
-
 Sus scrofa succinyl-Ala-Ala-Ala + 4-nitroaniline
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.36 8.5
-
-
 Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.36 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