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Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of <scene name='60/607865/Oxyanion_hole/1'>Gly-193 and Ser-195</scene> , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides. | Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of <scene name='60/607865/Oxyanion_hole/1'>Gly-193 and Ser-195</scene> , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides. | ||
The <scene name='60/607865/Asp_189/1'>aspartate residue</scene> located in the catalytic pocket of trypsin is responsible for attracting and stabilizing positively charged lysine or arginine, and as a result responsible for the specificity of the enzyme. | The <scene name='60/607865/Asp_189/1'>aspartate residue</scene> located in the catalytic pocket of trypsin is responsible for attracting and stabilizing positively charged lysine or arginine, and as a result responsible for the specificity of the enzyme <ref> doi:10.1021/pr0705035</ref>. | ||
Revision as of 14:27, 23 November 2014
TrypsinTrypsin
Trypsin is a serine protease, found in the digestive system of many vertebrates, where it hydrolyses proteins[1]. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin Break peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. FunctionTrypsin catalyzes the hydrolysis of peptide bonds and cutting proteins into smaller peptides in the duodenum. Structure and MechanismTrypsin is a medium size globular protein that contains either and . The enzymatic mechanism of Trypsin is similar to the other serine proteases. These enzymes contain a catalytic triad consisting of , These three residues form a charge relay that serves to make the active site serine nucleophilic [2]. Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides. The located in the catalytic pocket of trypsin is responsible for attracting and stabilizing positively charged lysine or arginine, and as a result responsible for the specificity of the enzyme [3].
Structural highlightsThere are different ways to present the protein structure,, and that show the protein from the N (blue) to C terminal (green)
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ReferencesReferences
- ↑ Rawlings ND, Barrett AJ. Families of serine peptidases. Methods Enzymol. 1994;244:19-61. doi: 10.1016/0076-6879(94)44004-2. PMID:7845208 doi:http://dx.doi.org/10.1016/0076-6879(94)44004-2
- ↑ Polgar L. The catalytic triad of serine peptidases. Cell Mol Life Sci. 2005 Oct;62(19-20):2161-72. PMID:16003488 doi:http://dx.doi.org/10.1007/s00018-005-5160-x
- ↑ Rodriguez J, Gupta N, Smith RD, Pevzner PA. Does trypsin cut before proline? J Proteome Res. 2008 Jan;7(1):300-5. Epub 2007 Dec 8. PMID:18067249 doi:http://dx.doi.org/10.1021/pr0705035