Sandbox Reserved 1851: Difference between revisions

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In the active state, there are two catalytic <scene name='10/1075253/Active_site_residues/6'>residues</scene> that aim to stabilize the transition state of the Diels-Alder reaction. Y134 acts as a <scene name='10/1075253/Ligand/5'>hydrogen bond donor</scene> to the oxygen on the <scene name='10/1075253/Ligand/2'>ligand</scene>. Q208 acts as a <scene name='10/1075253/Ligand/4'>hydrogen bond acceptor</scene> to the nitrogen on the ligand as well as a donor to the neighboring oxygen. These interactions help reduce the energetic gap between orbitals allowing the reaction to proceed, outlined in HOMO/LUMO.

===Helix Addition===

In the evolution process, researchers added a 16-residue <scene name='10/1075253/Helix/1'>a-helix motif</scene> to the top of the binding site. The hydrophobic helix “functions as a lid to constrain the substrates in a productive orientation for reaction” (CITE), decreasing the Km of the enzyme and increasing the catalytic efficiency, as seen in the measured kinetics of the enzyme.

In the evolution process, researchers added a 16-residue <scene name='10/1075253/Helix/2'>a-helix motif</scene> to the top of the binding site. The hydrophobic helix “functions as a lid to constrain the substrates in a productive orientation for reaction” (CITE), decreasing the Km of the enzyme and increasing the catalytic efficiency, as seen in the measured kinetics of the enzyme.

==Mechanism==

===Uncatalyzed Reaction===

Sandbox Reserved 1851: Difference between revisions

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@@ Line 9: / Line 9: @@
 In the active state, there are two catalytic <scene name='10/1075253/Active_site_residues/6'>residues</scene> that aim to stabilize the transition state of the Diels-Alder reaction. Y134 acts as a <scene name='10/1075253/Ligand/5'>hydrogen bond donor</scene> to the oxygen on the <scene name='10/1075253/Ligand/2'>ligand</scene>. Q208 acts as a <scene name='10/1075253/Ligand/4'>hydrogen bond acceptor</scene> to the nitrogen on the ligand as well as a donor to the neighboring oxygen. These interactions help reduce the energetic gap between orbitals allowing the reaction to proceed, outlined in HOMO/LUMO.
 ===Helix Addition===
-In the evolution process, researchers added a 16-residue <scene name='10/1075253/Helix/1'>a-helix motif</scene> to the top of the binding site. The hydrophobic helix “functions as a lid to constrain the substrates in a productive orientation for reaction” (CITE), decreasing the Km of the enzyme and increasing the catalytic efficiency, as seen in the measured kinetics of the enzyme.
+In the evolution process, researchers added a 16-residue <scene name='10/1075253/Helix/2'>a-helix motif</scene> to the top of the binding site. The hydrophobic helix “functions as a lid to constrain the substrates in a productive orientation for reaction” (CITE), decreasing the Km of the enzyme and increasing the catalytic efficiency, as seen in the measured kinetics of the enzyme.
 ==Mechanism==
 ===Uncatalyzed Reaction===