Team:Imperial College London/Stomach
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Contents |
Human Digestive Proteases:
- Pepsin = stomach
- Trypsin = duodenum
- Chymotrypsin
- Carboxypeptidase
Stomach
Pepsin
- Released by chief cells in the stomach.
- Expressed as a zymogen pepsinogen.
- Pepsinogen is converted to pepsin by HCl which is released by parietal cells of the stomach.
- Cleaves at the N-terminus after aromatic amino acids such as phenylalanine, tryptophan, and tyrosine.
- Optimum pH of 1.5 to 2. Pepsin denatures when the pH is more than 5.0.
Duodenum
Endopeptidases (trypsin, chymotryopsin, elastase)
Exopeptidases (carboxypeptidases A & B)
Enteropeptidase
Trypsin
Chymotryopsin
Elastase
Enterokinase
Carboxypeptidases A & B
Small Intestine = Aminopeptidase N
Dipeptidyl aminopeptidase IV
Aminopeptidase P
Carboxypeptidase P
Angotensin-converting enzyme
Glutamyl aminopeptidase
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PeptideCutter
PeptideCutter [references / documentation] predicts potential cleavage sites cleaved by proteases or chemicals in a given protein sequence. PeptideCutter returns the query sequence with the possible cleavage sites mapped on it and /or a table of cleavage site positions.