Sandbox Reserved 1709: Difference between revisions

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=== Active Site ===

Within the four transmembrane helices lies the <scene name='90/904314/Binding_pocket/1'>binding pocket</scene>. The binding pocket holds ~~two~~ <scene name='90/~~906893~~/Active_site/7'>two hydrophilic residues</scene> active site residues, N80 and Y139, that interact with the substrate. N80 and Y139 are surrounded by a <scene name='90/906893/Hydrophobic/3'>hydrophobic region</scene> that provides specificity to the region. The hydrophilic residues hydrogen bond to the substrate, providing recognition and increasing specificity. The <scene name='90/906893/Disulfide_-_132/1'>C132-C135 disulfide bridge</scene> above the binding pocket provides stabilization when a substrate is bound. This bridge provides increased stability for the binding site as it interacts with and binds substrates or inhibitors. The hydrophilic residues provide <scene name='90/906893/K_hbonds/1'>hydrogen bonds</scene> when interacting with substrates for specificity and recognition. Upon binding, VKOR will transition into the closed conformation allowing the catalytic mechanism to commence.

Within the four transmembrane helices lies the <scene name='90/904314/Binding_pocket/1'>binding pocket</scene>. The binding pocket holds <scene name='90/904314/Active_site/3'>two hydrophilic residues</scene> active site residues, N80 and Y139, that interact with the substrate. N80 and Y139 are surrounded by a <scene name='90/906893/Hydrophobic/3'>hydrophobic region</scene> that provides specificity to the region. The hydrophilic residues hydrogen bond to the substrate, providing recognition and increasing specificity. The <scene name='90/906893/Disulfide_-_132/1'>C132-C135 disulfide bridge</scene> above the binding pocket provides stabilization when a substrate is bound. This bridge provides increased stability for the binding site as it interacts with and binds substrates or inhibitors. The hydrophilic residues provide <scene name='90/906893/K_hbonds/1'>hydrogen bonds</scene> when interacting with substrates for specificity and recognition. Upon binding, VKOR will transition into the closed conformation allowing the catalytic mechanism to commence.

==Catalytic Mechanism of VKOR==

=== Brief Overview ===

The overall mechanism works to convert Vitamin K epoxide to an activated form of Vitamin K hydroquinone, as noted in Figure 1. The substrate will bind VKOR at the binding pocket in the <scene name='90/904314/Open_conformation/2'>open conformation</scene> and induce the <scene name='90/904314/Closed_conformation/5'>closed conformation</scene>. Initial transition from open to closed conformation occurs with the oxidation of the C43-C51 disulfide bridge. Here, VKOR will utilize the second pair of <scene name='90/904314/~~Disulfide_bridge_stabilization~~/7'>catalytic cysteines</scene>, C132 and C135, to reduce KO into Vitamin K and Vitamin K into KH2. KH2 will be released from the binding pocket fully activated and ready for use in the body. VKOR will reset by returning to the open conformation again and preparing for another substrate to bind.

The overall mechanism works to convert Vitamin K epoxide to an activated form of Vitamin K hydroquinone, as noted in Figure 1. The substrate will bind VKOR at the binding pocket in the <scene name='90/904314/Open_conformation/2'>open conformation</scene> and induce the <scene name='90/904314/Closed_conformation/5'>closed conformation</scene>. Initial transition from open to closed conformation occurs with the oxidation of the C43-C51 disulfide bridge. Here, VKOR will utilize the second pair of <scene name='90/904314/Disulfide_-_132/1'>catalytic cysteines</scene>, C132 and C135, to reduce KO into Vitamin K and Vitamin K into KH2. KH2 will be released from the binding pocket fully activated and ready for use in the body. VKOR will reset by returning to the open conformation again and preparing for another substrate to bind.

=== Enzymatic Mechanism ===

Sandbox Reserved 1709: Difference between revisions

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@@ Line 20: / Line 20: @@
 === Active Site ===
-Within the four transmembrane helices lies the <scene name='90/904314/Binding_pocket/1'>binding pocket</scene>. The binding pocket holds two <scene name='90/906893/Active_site/7'>two hydrophilic residues</scene> active site residues, N80 and Y139, that interact with the substrate. N80 and Y139 are surrounded by a <scene name='90/906893/Hydrophobic/3'>hydrophobic region</scene> that provides specificity to the region. The hydrophilic residues hydrogen bond to the substrate, providing recognition and increasing specificity. The <scene name='90/906893/Disulfide_-_132/1'>C132-C135 disulfide bridge</scene> above the binding pocket provides stabilization when a substrate is bound. This bridge provides increased stability for the binding site as it interacts with and binds substrates or inhibitors. The hydrophilic residues provide <scene name='90/906893/K_hbonds/1'>hydrogen bonds</scene> when interacting with substrates for specificity and recognition. Upon binding, VKOR will transition into the closed conformation allowing the catalytic mechanism to commence.
+Within the four transmembrane helices lies the <scene name='90/904314/Binding_pocket/1'>binding pocket</scene>. The binding pocket holds <scene name='90/904314/Active_site/3'>two hydrophilic residues</scene> active site residues, N80 and Y139, that interact with the substrate. N80 and Y139 are surrounded by a <scene name='90/906893/Hydrophobic/3'>hydrophobic region</scene> that provides specificity to the region. The hydrophilic residues hydrogen bond to the substrate, providing recognition and increasing specificity. The <scene name='90/906893/Disulfide_-_132/1'>C132-C135 disulfide bridge</scene> above the binding pocket provides stabilization when a substrate is bound. This bridge provides increased stability for the binding site as it interacts with and binds substrates or inhibitors. The hydrophilic residues provide <scene name='90/906893/K_hbonds/1'>hydrogen bonds</scene> when interacting with substrates for specificity and recognition. Upon binding, VKOR will transition into the closed conformation allowing the catalytic mechanism to commence.
 ==Catalytic Mechanism of VKOR==
 === Brief Overview ===
-The overall mechanism works to convert Vitamin K epoxide to an activated form of Vitamin K hydroquinone, as noted in Figure 1. The substrate will bind VKOR at the binding pocket in the <scene name='90/904314/Open_conformation/2'>open conformation</scene> and induce the <scene name='90/904314/Closed_conformation/5'>closed conformation</scene>. Initial transition from open to closed conformation occurs with the oxidation of the C43-C51 disulfide bridge. Here, VKOR will utilize the second pair of <scene name='90/904314/Disulfide_bridge_stabilization/7'>catalytic cysteines</scene>, C132 and C135, to reduce KO into Vitamin K and Vitamin K into KH2. KH2 will be released from the binding pocket fully activated and ready for use in the body. VKOR will reset by returning to the open conformation again and preparing for another substrate to bind.
+The overall mechanism works to convert Vitamin K epoxide to an activated form of Vitamin K hydroquinone, as noted in Figure 1. The substrate will bind VKOR at the binding pocket in the <scene name='90/904314/Open_conformation/2'>open conformation</scene> and induce the <scene name='90/904314/Closed_conformation/5'>closed conformation</scene>. Initial transition from open to closed conformation occurs with the oxidation of the C43-C51 disulfide bridge. Here, VKOR will utilize the second pair of <scene name='90/904314/Disulfide_-_132/1'>catalytic cysteines</scene>, C132 and C135, to reduce KO into Vitamin K and Vitamin K into KH2. KH2 will be released from the binding pocket fully activated and ready for use in the body. VKOR will reset by returning to the open conformation again and preparing for another substrate to bind.
 === Enzymatic Mechanism ===