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
-
3.4.21.1
-
pancreatic
-
elastase
-
proteinase
-
pepsin
-
pancreas
-
subtilisin
-
lipase
-
amylase
-
thrombin
-
exocrine
-
cathepsin
-
porcine
-
soybean
-
pronase
-
aureus
-
chymotryptic
-
plasmin
-
staphylococcus
-
erythrocyte
-
kallikrein
-
carboxypeptidase
-
thermolysin
-
bromide
-
trypsin-like
-
juice
-
bowman-birk
-
duodenal
-
cyanogen
-
edman
-
kunitz-type
-
collagenase
-
kunitz
-
midguts
-
zymogen
-
neuraminidase
-
serpins
-
cholecystokinin
-
trypsinogen
-
secretin
-
2-macroglobulin
-
chymase
-
bromelain
-
aprotinin
-
chloromethyl
-
p-nitroanilide
-
medicine
-
synthesis
-
gizzard
-
biotechnology
-
meromyosin
-
non-cholinergic
-
amidolytic
-
drug development
-
acyl-enzyme
-
agriculture
-
industry
- 3.4.21.1
- pancreatic
- elastase
- proteinase
- pepsin
- pancreas
- subtilisin
- lipase
- amylase
- thrombin
-
exocrine
- cathepsin
- porcine
- soybean
- pronase
- aureus
-
chymotryptic
- plasmin
- staphylococcus
- erythrocyte
- kallikrein
- carboxypeptidase
- thermolysin
- bromide
-
trypsin-like
- juice
-
bowman-birk
- duodenal
-
cyanogen
-
edman
-
kunitz-type
- collagenase
-
kunitz
- midguts
- zymogen
- neuraminidase
- serpins
- cholecystokinin
- trypsinogen
- secretin
-
2-macroglobulin
- chymase
- bromelain
- aprotinin
-
chloromethyl
- p-nitroanilide
- medicine
- synthesis
- gizzard
- biotechnology
- meromyosin
-
non-cholinergic
-
amidolytic
- drug development
- acyl-enzyme
- agriculture
- industry
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
3.4.21.1 chymotrypsinAdvanced search results
results (
results (Activating Compound
Activating Compound on EC 3.4.21.1 - chymotrypsin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1,2-propanediol
residual activity of bovine pancreatic alpha-chymotrypsin is studied in water/1,2-propanediol mixtures in the entire range of water content at 25°C. The degree of stabilization/ destabilization of alpha-chymotrypsin depends strongly on the water content in organic solvent. At high water content, the residual activity values are higher than 100%. At low water content, the residual catalytic activity is about 90-95%, compared with that observed after incubation in pure water
1,8-bis(tributylammonium)octane dibromide
provokes superactivation and stabilization effects in a way similar to cetyltributytetrabutylammonium bromide, but at lower concentration
benzyldodecyldimethylammonium bromide
increases activity instantaneously, but a deactivates the enzyme, faster than in pure buffer
benzyltributylammonium bromide
increases activity instantaneously, but a deactivates the enzyme, faster than in pure buffer
benzyltrimethylammonium bromide
increases activity instantaneously, but a deactivates the enzyme, faster than in pure buffer
hexadecyltrimethylammonium bromide
-
2-60 mM, aqueous micelles of the cationic polymeric surfactant hexadecyltrimethylammonium bromide
p-octyloxybenzyltributylammonium bromide
-
maximal activation at 5 mM, inhibition at extended incubation
selenium nanoparticles
immobilization of the enzyme on selenium nanoparticles increases the proteolytic activity of the enzyme, making it possible to efficiently operate at suboptimal pH values (in an alkaline medium)
-
silica
the activity of alpha-chymotrypsin is enhanced upon adsorption on silica particles. Pressure increases the activity of adsorbed alpha-chymotrypsin further
-
cetyltributylammonium bromide
provokes a superactivation of alpha-chymotrypsin in aqueous solution
dodecyltrimethylammonium bromide
in comparison to buffer the catalytic activity of the enzyme is enhanced 5fold in premicellar dodecyltrimethylammonium bromide solutions. Negligible changes are observed in cetyltrimethylammonium bromide and octadecyltrimethylammonium bromide
tetrabutylammonium bromide
provokes a superactivation of alpha-chymotrypsin in aqueous solution
additional information
-
15 min UV-A radiation reactivates 1-(2-nitrophenyl)ethanol coated enzyme
-
additional information
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. Results indicate that hydrophobic interactions were the driving force behind this aggregation
-
additional information
-
during purification, both chymotrypsin A and B are fully activated when extracted
-
