Sandbox wabash23
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
== Structural highlights == | == Structural highlights == | ||
| - | Trypsin's <scene name='72/725332/Specificity_pocet/2'>selectivity pocket</scene> selectively binds only positively charged residues such as Arg and Lys because the GLY 216 and 226 residues allows for the larger residues to fit in the pocket and are preferential because they stabilize the negative charge on the aspartic acid. The main transition state of interest of interest is the <scene name='72/725332/Acyl-intermediate/1'>acyl-intermediate</scene>which forms when the peptide bond of the newly bound substrate complex (as a tetrahedral intermediate) is cleaved yielding a carbonyl group on SER 195. The <scene name='72/725332/Active_site/1'>active site</scene> involves the residues SER 195, HIS 57, Asp 102 and GLY 193 in which the trypsin substrate forms a stable tetrahedral intermediate upon the formation of H-bonds located in what is known as the "oxyanion hole" which is located between SER 195 and GLY 193. This preferential binding of the enzyme-substrate complex of the acyl-enzyme intermediate is responsible for much of the catalytic efficiency of serine proteases. | + | Trypsin's <scene name='72/725332/Specificity_pocet/2'>selectivity pocket</scene> selectively binds only positively charged residues such as Arg and Lys because the GLY 216 and 226 residues allows for the larger residues to fit in the pocket and are preferential because they stabilize the negative charge on the aspartic acid. The main transition state of interest of interest is the <scene name='72/725332/Acyl-intermediate/1'>acyl-intermediate</scene> which forms when the peptide bond of the newly bound substrate complex (as a tetrahedral intermediate) is cleaved yielding a carbonyl group on SER 195. The <scene name='72/725332/Active_site/1'>active site</scene> involves the residues SER 195, HIS 57, Asp 102 and GLY 193 in which the trypsin substrate forms a stable tetrahedral intermediate upon the formation of H-bonds located in what is known as the "oxyanion hole" which is located between SER 195 and GLY 193. This preferential binding of the enzyme-substrate complex of the acyl-enzyme intermediate is responsible for much of the catalytic efficiency of serine proteases. |
Current revision
The Mechanism of Trypsin
| |||||||||||
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
- ↑ 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
