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 (Application
Application 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
APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
-
chymotrypsin and potentially other serine proteases could be attractive candidates for the development of biocatalyst for the control of residual pesticides in the environment and on agricultural products
biotechnology
-
dependence of activity on pH and temperature makes chymotrypsin II a biotechnological alternative for food processing when low temperatures are needed like in fish ripening, fish sauce production, fish protein hydrolysate production and other emerging processes. This enzyme together with other proteases from sardine viscera may aid in the enzymatic treatment of stick-water, in which a reduction in viscosity is required for further processing of effluent
drug development
industry
medicine
synthesis
additional information
-
potential application value of the two chymotrypsins A and B where low processing temperature and higher enzymatic activity is needed
drug development
-
design of a new class of boron peptides as inhibitors of the chymotrypsin-like activity of the 20S proteasome based around the structure of Belactosin C, proteasome inhibitors with therapeutic utility
drug development
enediyne-amino acid conjugates as potent inhibitors of alpha-chymotrypsin
drug development
-
G-quadruplex-scaffold-based receptors are effective inhibitors of ChT by protein-surface recognition. This may provide a general strategy to generate synthetic combinatorial libraries of receptors to target different classes of proteins
drug development
-
winged bean chymotrypsin-trypsin inhibitor is a dual inhibitor of both chymotrypsin and trypsin and a promising candidate to study for its insecticidal properties against Helicoverpa armigera and other insect pests
industry
-
the enzyme is successfully immobilized on a non-leaching material surface to provide a new material able to inhibit biofilm colonization. The multiple-target nature of the protease activity allows the new material to be used with a broad-spectrum activity against polymicrobial infections, including drug-resistant strains
industry
-
the enzyme possesses potential applications in the food, leather and silk industries where acidic or slightly alkaline conditions are needed
industry
-
the enzyme is successfully immobilized on a non-leaching material surface to provide a new material able to inhibit biofilm colonization. The multiple-target nature of the protease activity allows the new material to be used with a broad-spectrum activity against polymicrobial infections, including drug-resistant strains
-
medicine
-
study of the clinical utility of trypsin/chymotrypsin combination in tissue repair. Trypsin/chymotrypsin oral combination is a promising treatment to facilitate healing of traumatic injuries. It promotes speedier recovery and better resolution of inflammatory signs and symptoms due to tissue injury than several of the other existing enzyme preparations. It demonstrates analgesic effects and reduces pain associated with healing. The trypsin/chymotrypsin combination shows efficacy and safety in accidental injuries, surgical and orthopedic injuries, burns, and sciatica
medicine
-
the enzyme is successfully immobilized on a non-leaching material surface to provide a new material able to inhibit biofilm colonization. The multiple-target nature of the protease activity allows the new material to be used with a broad-spectrum activity against polymicrobial infections, including drug-resistant strains
medicine
-
the enzyme is successfully immobilized on a non-leaching material surface to provide a new material able to inhibit biofilm colonization. The multiple-target nature of the protease activity allows the new material to be used with a broad-spectrum activity against polymicrobial infections, including drug-resistant strains
-
synthesis
-
enzymes are often used in organic solvents for catalyzing organic synthesis. Two enzyme preparations, EPRP (enzyme precipitated and rinsed with n-propanol) and PCMC (protein coated microcrystals) show much higher activities than lyophilized powders in such systems. Both preparations involve precipitation by an organic solvent
synthesis
construction of three different molecular weight multimodal temperature-responsive chymotrypsin-poly(sulfobetaine methacrylamide)-block-poly(N-isopropylacrylamide) protein-polymer conjugates that respond structurally to both low and high temperature. In the block copolymer grown from the surface of the enzyme, upper critical solution temperature phase transition is dependent on the chain length of the polymers in the conjugates, whereas lower critical solution temperature phase transition is independent of molecular weight. Each protein conjugate shows temperature dependent changes in substrate affinity and productivity when assayed from 0 to 40°C. The conjugates show higher stability to harsh conditions, including temperature, low pH, and protease degradation. The modified enzyme is active for over 8 h in the presence of a stomach protease at pH 1.0
synthesis
use of immobilized bovine alpha-chymotrypsin in a biotransformation process applying an aqueous micellar two-phase system for separation and recycling of the enzyme immobilisates. The thermoresponsive surfactant, Eumulgin ES, has no influence on the activity up to a concentration of 10%, while surfactants Tween 20, Triton X 114, Triton X 100 lead to an activity reduction. For Triton X-114, the activity rises to its previous value after washing or a buffer exchange influence. Optimization of the aqueous micellar two-phase system composition via a Design of Experiments approach allows for reuse of the immobilisates for hemoglobin digestion over eleven cycles in an Eumulgin ES aqueous micellar two-phase system
