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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

Metals Ions

Metals Ions on EC 3.4.21.1 - chymotrypsin

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
CdCl2 binds to the enzyme mainly via electrostatic forces with binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosens the protein skeleton and increases the molecular volume of the enzyme. CdCl2 first binds to the interface of the enzyme and then interacts with the key residues His57 or Asp102 or both in the active sites, leading to the activity inhibition of the enzyme under the exposure of high CdCl2 concentrations