Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
Function:
CTRB1 (Chymotrypsinogen B1) is the inactive precursor of Alpha chymotrypsin, one of a family of serine proteases secreted into the gastrointestinal tract. The zymogen is activated by proteolytic cleavage by trypsin.
Subcellular Location:
Secreted, extracellular space.
Similarity:
Belongs to the peptidase S1 family.
Contains 1 peptidase S1 domain.
SWISS:
P17538
Gene ID:
1504
Database links:
Entrez Gene: 1504 Human
Entrez Gene: 66473 Mouse
Entrez Gene: 24291 Rat
Omim: 118890 Human
SwissProt: P17538 Human
SwissProt: Q9CR35 Mouse
SwissProt: P07338 Rat
|
|
