Trypsin: Difference between revisions

Line 23:

[[Image:Ligandinteractionstrypsin.gif|thumb|left|upright=2.5|A two-dimensional representation of trypsin binding Ligand UB-THR 10]]

The <scene name='~~Sandbox_45~~/~~Ctriadd102h57s195~~/4'>catalytic triad</scene>; Asp 102, His 57, and Ser 195, shown here in yellow, is positioned near the substrate. The catalytically active histidine and serine side chains are even near an amide bond in UB-THR 10, just like the amide bond broken in peptide hydrolysis. According to FirstGlance in Jmol, there is no bonding of these groups with the ligand, apart from minor van der Waal's interactions with Hist 57. If Ligand UB-Thr 10 were a transition state analog, some covalent connection would exist in addition to hydrogen bonds. UB-THR 10 simulates the substrate, but does not hydrolyze at either of its two amide bonds, likely due to the local cyclic groups atypical of peptide backbones.

The <scene name='10/100160/Cv/6'>catalytic triad</scene>; Asp 102, His 57, and Ser 195, shown here in yellow, is positioned near the substrate. The catalytically active histidine and serine side chains are even near an amide bond in UB-THR 10, just like the amide bond broken in peptide hydrolysis. According to FirstGlance in Jmol, there is no bonding of these groups with the ligand, apart from minor van der Waal's interactions with Hist 57. If Ligand UB-Thr 10 were a transition state analog, some covalent connection would exist in addition to hydrogen bonds. UB-THR 10 simulates the substrate, but does not hydrolyze at either of its two amide bonds, likely due to the local cyclic groups atypical of peptide backbones.

==Regulation==

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 23: / Line 23: @@
 [[Image:Ligandinteractionstrypsin.gif|thumb|left|upright=2.5|A two-dimensional representation of trypsin binding Ligand UB-THR 10]]
 {{Clear}}
-The <scene name='Sandbox_45/Ctriadd102h57s195/4'>catalytic triad</scene>; Asp 102, His 57, and Ser 195, shown here in yellow, is positioned near the substrate. The catalytically active histidine and serine side chains are even near an amide bond in UB-THR 10, just like the amide bond broken in peptide hydrolysis.  According to FirstGlance in Jmol, there is no bonding of these groups with the ligand, apart from minor van der Waal's interactions with Hist 57.  If Ligand UB-Thr 10 were a transition state analog, some covalent connection would exist in addition to hydrogen bonds. UB-THR 10 simulates the substrate, but does not hydrolyze at either of its two amide bonds, likely due to the local cyclic groups atypical of peptide backbones.
+The <scene name='10/100160/Cv/6'>catalytic triad</scene>; Asp 102, His 57, and Ser 195, shown here in yellow, is positioned near the substrate. The catalytically active histidine and serine side chains are even near an amide bond in UB-THR 10, just like the amide bond broken in peptide hydrolysis.  According to FirstGlance in Jmol, there is no bonding of these groups with the ligand, apart from minor van der Waal's interactions with Hist 57.  If Ligand UB-Thr 10 were a transition state analog, some covalent connection would exist in addition to hydrogen bonds. UB-THR 10 simulates the substrate, but does not hydrolyze at either of its two amide bonds, likely due to the local cyclic groups atypical of peptide backbones.
 ==Regulation==