Sandbox Wabash3
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==Mechanism of Trypsin== | ==Mechanism of Trypsin== | ||
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | Trypsin is serine protease which catalyzes the hydrolysis of peptide bonds of a substrate via an acylation reaction and a deacylation reaction. In the first (acylation) reaction, the nucleophilic serine attacks the substrate scissile bond, forming a tetrahedral intermediate and then a covalent acyl-enzyme with the release of the C-terminal fragment. In the second (deacylation) reaction, a water molecule attacks the acyl-enzyme, leading to a second tetrahedral intermediate followed by release of the N-terminal fragment. The specificity of substrates is determined by the structure of its active site, which contains Ser-195, His-57, and Asp-189. <scene name='72/725340/Asp_189/2'>TextToBeDisplayed</scene> (Asp189 '''Sandbox Wabash3'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | + | Trypsin is serine protease which catalyzes the hydrolysis of peptide bonds of a substrate via an acylation reaction and a deacylation reaction. In the first (acylation) reaction, the nucleophilic serine attacks the substrate scissile bond, forming a tetrahedral intermediate and then a covalent acyl-enzyme with the release of the C-terminal fragment. In the second (deacylation) reaction, a water molecule attacks the acyl-enzyme, leading to a second tetrahedral intermediate followed by release of the N-terminal fragment. The specificity of substrates is determined by the structure of its active site, which contains Ser-195, <scene name='72/725340/His-57/1'>His57</scene>, and Asp-189. <scene name='72/725340/Asp_189/2'>TextToBeDisplayed</scene> (Asp189 '''Sandbox Wabash3'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. |
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
Revision as of 23:58, 14 February 2016
Mechanism of Trypsin
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Radisky ES, Lee JM, Lu CJ, Koshland DE Jr. Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277
