Sandbox Reserved 1724: Difference between revisions

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{{Template:CH462_Biochemistry_II_2022}}

<scene name='90/904329/Cat_cycle_3/4'>Text To Be Displayed</scene>{{Template:CH462_Biochemistry_II_2022}}

==Vitamin K Epoxide Reductase==

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===Overview===

The catalytic cycle shows how vitamin K epoxide reductase structurally transforms from an open wild type conformation to having several different types of substrates within its binding pocket. The first step of the catalytic cycle of shown to the right is the <scene name='90/904329/Cat_cycle_i/1'>wild type open conformation</scene>, labeled I. This step is characterized by an open cap domain with a disulfide bond (43-51) and a second disulfide bond (132-135) in the alpha helices. As shown this step can be characterized as closed when warfarin sits within the binding pocket without the disulfide bonds changing so that the cap domain does not actually close. This step is considered closed because vitamin K would not be able to enter the binding pocket in any of its forms. The second step of the catalytic cycle is a <scene name='90/904329/Cat_cycle_2/1'>closed conformation</scene> labeled II. This step is characterized by a disulfide bond between the cap domain and alpha helices (51 and 132), with both containing an SH group. Warfarin can sit within this structure without disrupting and of these sulfur groups. The next step of the cycle, <scene name='90/904329/Cat_cycle_3/3'>~~labeled~~ III</scene>, is slightly different because KOH or KH (depending on the step of the vitamin K cycle) binds to the cysteine 135 within the alpha helices. This is also a closed structure. Lastly, structure IV of the catalytic cycle is also a closed structure. The major difference is the orientation of the disulfide and cysteine interactions.

The catalytic cycle shows how vitamin K epoxide reductase structurally transforms from an open wild type conformation to having several different types of substrates within its binding pocket. The first step of the catalytic cycle of shown to the right is the <scene name='90/904329/Cat_cycle_i/1'>wild type open conformation</scene>, labeled I. This step is characterized by an open cap domain with a disulfide bond (43-51) and a second disulfide bond (132-135) in the alpha helices. As shown this step can be characterized as closed when warfarin sits within the binding pocket without the disulfide bonds changing so that the cap domain does not actually close. This step is considered closed because vitamin K would not be able to enter the binding pocket in any of its forms. The second step of the catalytic cycle is a <scene name='90/904329/Cat_cycle_2/1'>closed conformation</scene> labeled II. This step is characterized by a disulfide bond between the cap domain and alpha helices (51 and 132), with both containing an SH group. Warfarin can sit within this structure without disrupting and of these sulfur groups. The next step of the cycle, labeled <scene name='90/904329/Cat_cycle_3/4'>III</scene>, is slightly different because KOH or KH (depending on the step of the vitamin K cycle) binds to the cysteine 135 within the alpha helices. This is also a closed structure. Lastly, structure IV of the catalytic cycle is also a closed structure. The major difference is the orientation of the disulfide and cysteine interactions.

===Catalytic Cysteines===

Sandbox Reserved 1724: Difference between revisions

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-{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
+<scene name='90/904329/Cat_cycle_3/4'>Text To Be Displayed</scene>{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
 ==Vitamin K Epoxide Reductase==
 <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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 ===Overview===
-The catalytic cycle shows how vitamin K epoxide reductase structurally transforms from an open wild type conformation to having several different types of substrates within its binding pocket. The first step of the catalytic cycle of shown to the right is the <scene name='90/904329/Cat_cycle_i/1'>wild type open conformation</scene>, labeled I. This step is characterized by an open cap domain with a disulfide bond (43-51) and a second disulfide bond (132-135) in the alpha helices. As shown this step can be characterized as closed when warfarin sits within the binding pocket without the disulfide bonds changing so that the cap domain does not actually close. This step is considered closed because vitamin K would not be able to enter the binding pocket in any of its forms. The second step of the catalytic cycle is a <scene name='90/904329/Cat_cycle_2/1'>closed conformation</scene> labeled II. This step is characterized by a disulfide bond between the cap domain and alpha helices (51 and 132), with both containing an SH group. Warfarin can sit within this structure without disrupting and of these sulfur groups. The next step of the cycle, <scene name='90/904329/Cat_cycle_3/3'>labeled III</scene>, is slightly different because KOH or KH (depending on the step of the vitamin K cycle) binds to the cysteine 135 within the alpha helices. This is also a closed structure. Lastly, structure IV of the catalytic cycle is also a closed structure. The major difference is the orientation of the disulfide and cysteine interactions.
+The catalytic cycle shows how vitamin K epoxide reductase structurally transforms from an open wild type conformation to having several different types of substrates within its binding pocket. The first step of the catalytic cycle of shown to the right is the <scene name='90/904329/Cat_cycle_i/1'>wild type open conformation</scene>, labeled I. This step is characterized by an open cap domain with a disulfide bond (43-51) and a second disulfide bond (132-135) in the alpha helices. As shown this step can be characterized as closed when warfarin sits within the binding pocket without the disulfide bonds changing so that the cap domain does not actually close. This step is considered closed because vitamin K would not be able to enter the binding pocket in any of its forms. The second step of the catalytic cycle is a <scene name='90/904329/Cat_cycle_2/1'>closed conformation</scene> labeled II. This step is characterized by a disulfide bond between the cap domain and alpha helices (51 and 132), with both containing an SH group. Warfarin can sit within this structure without disrupting and of these sulfur groups. The next step of the cycle, labeled <scene name='90/904329/Cat_cycle_3/4'>III</scene>, is slightly different because KOH or KH (depending on the step of the vitamin K cycle) binds to the cysteine 135 within the alpha helices. This is also a closed structure. Lastly, structure IV of the catalytic cycle is also a closed structure. The major difference is the orientation of the disulfide and cysteine interactions.
 ===Catalytic Cysteines===