"
Team:Imperial College London/Stomach
From 2009.igem.org
(Difference between revisions)
(→Peptide cutter) |
(→Peptide cutter) |
||
| Line 64: | Line 64: | ||
<input type=hidden name=enzyme value=Pn1.3 checked> | <input type=hidden name=enzyme value=Pn1.3 checked> | ||
<input type=hidden checked name=cleavage_map value=cleavage_map> | <input type=hidden checked name=cleavage_map value=cleavage_map> | ||
| - | |||
| - | |||
| - | |||
| - | |||
| - | |||
| - | |||
| - | |||
| - | |||
<input type=hidden name=alphtable checked value=alphtable> | <input type=hidden name=alphtable checked value=alphtable> | ||
<input type=hidden name=cleave_number checked value=all> | <input type=hidden name=cleave_number checked value=all> | ||
Revision as of 10:51, 2 October 2009
Contents |
Human Digestive Proteases:
The stomach serves to break large proteins into peptides. These peptides are then broken down into amino acids once they enter the duodenum.
- Pepsin = stomach
- Trypsin = duodenum
- Chymotrypsin
- Carboxypeptidase
Stomach
The stomach is the first point at which polypeptides are broken down. The low pH of the stomach causes enzymes to denature, opening them up to attack from proteases such as pepsin.
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.
Peptide cutter
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.
