Sandbox Reserved 1846: Difference between revisions

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=== F243 ===

The original residue at <scene name='10/1075247/Better_f234/3'>F243</scene> was ~~also~~ mutated. This residue is located 3.6 Å from the ligand. Two mutations at this position, <scene name='10/1075247/Better_f243i/2'>F243I</scene> and F243W, increase the catalytic activity of the enzyme. The F243I mutation replaces Phe with Ile, a smaller side chain that allows the ligand to sit closer. This reduces the ligand distance to 3.0 Å. This tighter interaction improves substrate binding. The F243W mutation contains Trp, which has a bulkier, nitrogen-containing aromatic side chain. Trp brings the ligand slightly closer at 3.2 Å and introduces potential for new interactions, such as hydrogen bonding or [https://en.wikipedia.org/wiki/Pi-stacking#:~:text=In%20chemistry%2C%20pi%20stacking%20(also,interaction%22)%20is%20electrostatically%20repulsive. π-stacking]. Both mutations result in improved catalytic performance. The F243I mutant shows a 27.5% increase in activity, while the F243W mutant shows a 17.5% increase, compared to the wild-type enzyme.<ref name="Tournier"/>

The original residue at <scene name='10/1075247/Better_f234/3'>F243</scene> was mutated. This residue is located 3.6 Å from the ligand. Two mutations at this position, <scene name='10/1075247/Better_f243i/2'>F243I</scene> and F243W, increase the catalytic activity of the enzyme. The F243I mutation replaces Phe with Ile, a smaller side chain that allows the ligand to sit closer. This reduces the ligand distance to 3.0 Å. This tighter interaction improves substrate binding. The F243W mutation contains Trp, which has a bulkier, nitrogen-containing aromatic side chain. Trp brings the ligand slightly closer at 3.2 Å and introduces potential for new interactions, such as hydrogen bonding or [https://en.wikipedia.org/wiki/Pi-stacking#:~:text=In%20chemistry%2C%20pi%20stacking%20(also,interaction%22)%20is%20electrostatically%20repulsive. π-stacking]. Both mutations result in improved catalytic performance. The F243I mutant shows a 27.5% increase in activity, while the F243W mutant shows a 17.5% increase, compared to the wild-type enzyme.<ref name="Tournier"/>

=== Y127 ===

Sandbox Reserved 1846: Difference between revisions

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@@ Line 43: / Line 43: @@
 === F243 ===
-The original residue at <scene name='10/1075247/Better_f234/3'>F243</scene> was also mutated. This residue is located 3.6 Å from the ligand. Two mutations at this position, <scene name='10/1075247/Better_f243i/2'>F243I</scene> and F243W, increase the catalytic activity of the enzyme. The F243I mutation replaces Phe with Ile, a smaller side chain that allows the ligand to sit closer. This reduces the ligand distance to 3.0 Å. This tighter interaction improves substrate binding. The F243W mutation contains Trp, which has a bulkier, nitrogen-containing aromatic side chain. Trp brings the ligand slightly closer at 3.2 Å and introduces potential for new interactions, such as hydrogen bonding or [https://en.wikipedia.org/wiki/Pi-stacking#:~:text=In%20chemistry%2C%20pi%20stacking%20(also,interaction%22)%20is%20electrostatically%20repulsive. π-stacking]. Both mutations result in improved catalytic performance. The F243I mutant shows a 27.5% increase in activity, while the F243W mutant shows a 17.5% increase, compared to the wild-type enzyme.<ref name="Tournier"/>
+The original residue at <scene name='10/1075247/Better_f234/3'>F243</scene> was mutated. This residue is located 3.6 Å from the ligand. Two mutations at this position, <scene name='10/1075247/Better_f243i/2'>F243I</scene> and F243W, increase the catalytic activity of the enzyme. The F243I mutation replaces Phe with Ile, a smaller side chain that allows the ligand to sit closer. This reduces the ligand distance to 3.0 Å. This tighter interaction improves substrate binding. The F243W mutation contains Trp, which has a bulkier, nitrogen-containing aromatic side chain. Trp brings the ligand slightly closer at 3.2 Å and introduces potential for new interactions, such as hydrogen bonding or [https://en.wikipedia.org/wiki/Pi-stacking#:~:text=In%20chemistry%2C%20pi%20stacking%20(also,interaction%22)%20is%20electrostatically%20repulsive. π-stacking]. Both mutations result in improved catalytic performance. The F243I mutant shows a 27.5% increase in activity, while the F243W mutant shows a 17.5% increase, compared to the wild-type enzyme.<ref name="Tournier"/>
 === Y127 ===