3.4.21.1: chymotrypsin

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

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

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Results	in table
24	Activating Compound
103	AA Sequence
19	Application
1	CAS Registry Number
7	Cloned(Commentary)
14	Crystallization (Commentary)
1998	Disease/ Diagnostics
5	General Information
11	General Stability
45	IC50 Value
335	Inhibitors
44	kcat/KM [mM/s]
115	Ki Value [mM]
189	KM Value [mM]
5	Localization
11	Metals/Ions
35	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
14	Organic Solvent Stability
199	Organism
245	PDB ID
31	pH Optimum
16	pH Range
17	pH Stability
10	pI Value
8	Posttranslational Modification
5	Protein Variants
32	Purification (Commentary)
2	Reaction
1	Reaction Type
172	Reference
113	Source Tissue
33	Specific Activity [micromol/min/mg]
6	Storage Stability
250	Substrates and Products (Substrate)
19	Subunits
148	Synonyms
16	Temperature Optimum [°C]
11	Temperature Range [°C]
27	Temperature Stability [°C]
187	Turnover Number [1/s]

Organic Solvent Stability

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Organic Solvent Stability on EC 3.4.21.1 - chymotrypsin

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ORGANIC SOLVENT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

acetonitrile

Bos taurus

-

approx. 50% loss of activity after 20 min at 25°C in 70% acetonitrile, complete loss of activity after 20 min at 25°C in 75% acetonitrile, approx. 40% loss of activity after 20 min at 25°C in 95% acetonitrile

649560

dimethyl sulfoxide

Bos taurus

P00766

study on the influence of different water-dimethyl sulfoxide mixtures encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/n-heptane reverse micelles on the enzymatic hydrolysis of N-benzoyl-L-tyrosine p-nitroanilide by alpha-chymotrypsin. The enzyme dissolved in a 20% molar ratio of the dimethyl sulfoxide-water mixture does not present enzymatic activity. There is preferential solvation of the 1,4-bis-2-ethylhexylsulfosuccinate reverse micelle interface by water molecules. The kinetic parameters are determined at fixed ratio ([water] + [dimethyl sulfoxide])/[1,4-bis-2-ethylhexylsulfosuccinate] = 20 at different dimethyl sulfoxide-water compositions. Michaelis-Menten mechanism is valid for alpha-chymotrypsin in all the reverse micelle systems studied and the reaction takes place at the reverse micelle interface. The enzyme encapsulated by the reverse micelles shows catalytic effects with similar kcat/KM values at any dimethyl sulfoxide composition investigated

732430

dioxane

Bos taurus

-

approx. 50% loss of activity after 20 min at 25°C in 20% 1,4-dioxane, complete loss of activity after 20 min at 25°C in 60% 1,4-dioxane, approx. 80% loss of activity after 20 min at 25°C in 95% 1,4-dioxane

649560

Ethanol

5 entries

tert-Butanol

Bos taurus

P00766

precipitation of alpha-chymotrypsin in the simultaneous presence of ammonium sulfate and tert-butanol, i.e. three phase partitioning, results in preparations which show self aggregation of the enzyme molecules. The aggregates have irregular shapes and have about 3fold higher catalytic activity than the native enzyme. The aggregates do not differ in lambdamax of fluorescence emission, which is around 340 nm. All the aggregates show higher fluorescence emission intensity. Far-UV and near-UV circular dichroism also show no significant structural changes as compared to the native molecule. HPLC gel filtration gives 14 nm as the diameter for all preparations. Results indicate that hydrophobic interactions were the driving force behind this aggregation

732711

additional information

5 entries

Ethanol

Bos taurus

-

almost complete loss of activity after 10 min in 60% ethanol, no decrease in activity in the presence of 1.2 M CaCl2

649617

Ethanol

Bos taurus

-

approx. 50% loss of activity after 20 min at 25°C in 20% ethanol, complete loss of activity after 20 min at 25°C in 40% ethanol, approx. 60% loss of activity after 20 min at 25°C in 95% ethanol

649560

Ethanol

Bos taurus

-

approx. 50% loss of activity after 5 min at 25°C in 60% ethanol, almost complete loss of activity after 10 min, approx. 50% loss of activity after 10 min at 25°C in 50% ethanol, approx. 50% loss of activity after 15 min at 25°C in 40% ethanol, approx. 30% loss of activity after 40 min at 25°C in 30% ethanol, no loss of activity after 120 min at 25°C in 60% ethanol in the presence of 100 mg/ml polyethylene glycol 2000, approx. 50% loss of activity after 120 min at 25°C in 60% ethanol in the presence of 1.4 M D-fructose, 1.24 M D-sorbitol, 700 mM saccharose, or 12.5% glycerol

649596

Ethanol

Bos taurus

-

approx. 60% loss of activity after 20 min in 40% ethanol, complete loss of activity after 20 min in 60% ethanol, 70% loss of activity after 60 min in 60% ethanol in the presence of polyethylene glycol 6000, 12000 or 20000

649638

Ethanol

Bos taurus

-

at 50% ethanol alpha-chymotrypsin has an ordinary beta-sheet structure, at 70% or 90% ethanol the structure changes to a native-like, i.e. alpha and beta type, structure

650617

additional information

Bos taurus

P00766

effect of cationic surfactants cetyltriphenylphosphonium bromide, cetyltributylphosphonium bromide and cetyltrimethylammonium bromide on the hydrolysis of 4-nitrophenyl benzoate catalyzed by alpha-chymotrypsin. The ester is hydrolyzed readily in all the surfactants with the highest activity shown in cetyltributylphosphonium bromide

732428

additional information

Bos taurus

P00766

hydrolysis of 4-nitrophenyl acetate catalysed by alpha-chymotrypsin in sodium 1,4-bis(2-ethylhexyl)sulfosuccinate/isooctane/buffer reverse micelles. The increase in alpha-chymotrypsin activity and stability is an optimum at [H2O]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 10, and [isooctane]/[sodium 1,4-bis(2-ethylhexyl)sulfosuccinate] = 5

732228

additional information

Bos taurus

P00766

interactions among cetyltriphenylphosphonium bromide with alpha-chymotrypsin in aqueous medium at pH 7.75. With increasing concentration of alpha-chymotrypsin, the critical micellar concentration value of cetyltriphenylphosphonium bromide increases indicating strong interaction between cetyltriphenylphosphonium bromide and enzyme. The fluorescence intensity of alpha-chymotrypsin decreases on increasing concentration of cetyltriphenylphosphonium bromide. In cetyltriphenylphosphonium bromide micelle media, emission bands of tryptophan residues of alpha-chymotrypsin are blue shifted from 337 to 342 nm at pH 7.75

731677

additional information

Bos taurus

P00766

kinetic evaluation of alpha-chymotrypsin activity in cetyltrimethylammonium bromide/ionic liquid mixed micelles and development of an automatic methodology, based on sequential injection analysis. cetyltrimethylammonium bromide/ionic liquids mixed micellar systems can induce alpha-chymotrypsin superactivity. CMC and average micellar size of cetyltrimethylammonium bromide/1-hexyl-3-methylimidazolium chloride, cetyltrimethylammonium bromide/1-butyl-3-methylimidazoliumchloride, cetyltrimethylammonium bromide/1-butyl-1-methylpyrrolidinium and cetyltrimethylammonium bromide/1-butyl-4-methylpyridinium chloride mixed micelles were evaluated by fluorescence and dynamic light scattering, respectively. The sequential injection analysis methodology is suitable for evaluation of alpha-chymotrypsin activity in mixed micelles as it proves to be robust and exhibits good repeatability in all the assay conditions

731678

additional information

Bos taurus

P00766

supramolecular complexes of alpha-chymotrypsin with hydroxyl-containing alkyl ammonium gemini surfactants, i.e. alpha,omega-alkanedyl-bis(hydroxyethylmethylcetyl ammonium dibromides), with a polymethylene spacer of varying length. The interaction of the surfactants with alpha-chymotrypsin leads to changes of different intensity in the structural state of proteins. A correlation is found between the activity of alpha-chymotrypsin and the length of the spacer moiety. The enzyme activity correlates with the change in the substrate concentration in the aqueous phase of the surfactant micellar solution

732398