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3.4.21.1: chymotrypsin

This is an abbreviated version!
For detailed information about chymotrypsin, go to the full flat file.

Word Map on EC 3.4.21.1

Reaction

Preferential cleavage: Tyr-/-, Trp-/-, Phe-/-, Leu-/- =

Synonyms

4CHA, Alcalase, alpha chymar, alpha chymotrypsin, alpha-Chy, alpha-chymar ophth, alpha-chymotrypsin, alpha-chymotrypsin A, alpha-CT, avazyme, bovine alpha-chymotrypsin, caldecrin, cationic chymotrypsin, cellulomonadin, CHT, Chtp, Chtr1, Chtr2, Chtr3, Chtr4, ChTRP, CHY1, CHY20, chymar, chymotest, chymotrypsin, chymotrypsin A, chymotrypsin B, chymotrypsin C, chymotrypsin C1, chymotrypsin I, chymotrypsin II, chymotrypsin isoform Kh1, chymotrypsin isoform Kh2, chymotrypsin isoform Kh3, chymotrypsin-B, CTRA, Ctrb, EC 3.4.4.5, EC 3.4.4.6, enzeon, LBCP, lysosomal Bid cleavage protease, PEG-alpha-chymotrypsin, PEG-modified alpha-chymotrypsin, quimar, quimotrase, serine protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.1 chymotrypsin

General Stability

General Stability on EC 3.4.21.1 - chymotrypsin

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1,8-bis(tributylammonium)octane dibromide provokes stabilization effects in a way similar to cetyltributytetrabutylammonium bromide, but at lower concentration
alpha-chymotrypsin immobilized on mesoporous silica is stable for at least 1 week, i.e. 20 recycles per day, at room temperature, activity decreases gradually to 15% during next 10 days
-
autolysis of alpha-chymotrypsin is impeded when the enzyme is adsorbed on silica particles
Ca2+ stabilizes the enzyme near pH 7, at low pH the enzyme is more stable in absence of Ca2+
-
enzyme stability is analyzed in 0.05 M Tris-HCl buffer pH 8.20 in the presence or the absence of methylamine, urea or methylamine + urea mixture of various concentrations at 25°C for 4 h to attain complete equilibrium. Indication that methylamines suppress the aggregation of a thermal denatured protein and that methylamines have comparable effects on counteracting the temperature-perturbing actions on alpha-chymotrypsin.
immobilization of the enzyme on selenium nanoparticles increases the stability
in the presence of putrescine and spermidine a clear stabilizing effect against thermal unfolding is achieved
-
lanthanide ions, e.g. terbium accelerates the inactivation process
-
protects the enzyme from inactivation process, probably of autolytic nature
-
stability of the enzyme is increased in the presence of spermine
the enzyme becomes more stable in the presence of L-Met, based on the molecular dynamics simulation