Sandbox Reserved 1709: Difference between revisions
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== Introduction== | == Introduction== | ||
=== | === Biological Role of VKOR === | ||
<scene name='90/906893/Vkor_structure/1'>Vitamin K epoxide reductase</scene> (VKOR) is an enzyme that, as its name implies, promotes the reduction of <scene name='90/906893/Vkor_with_ko/1'>vitamin K epoxide</scene> (KO). VKOR is a transmembrane protein spanning the endoplasmic reticulum and composed of [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919313/ 4 transmembrane helical proteins]. One of its primary roles is to assist in blood coagulation by regenerating hydroquinone (KH2). KH2 acts as a γ-carboxylase cofactor that drives the γ-carboxylation of several coagulation factors. Structural characterization of VKOR has been difficult, though, due to its in vitro instability. Nonetheless, a near perfect atomic structure has been determined utilization anticoagulant stabilization and VKOR-like [https://pubmed.ncbi.nlm.nih.gov/33154105/ homologs]. | <scene name='90/906893/Vkor_structure/1'>Vitamin K epoxide reductase</scene> (VKOR) is an enzyme that, as its name implies, promotes the reduction of <scene name='90/906893/Vkor_with_ko/1'>vitamin K epoxide</scene> (KO). VKOR is a transmembrane protein spanning the endoplasmic reticulum and composed of [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919313/ 4 transmembrane helical proteins]. One of its primary roles is to assist in blood coagulation by regenerating hydroquinone (KH2). KH2 acts as a γ-carboxylase cofactor that drives the γ-carboxylation of several coagulation factors. Structural characterization of VKOR has been difficult, though, due to its in vitro instability. Nonetheless, a near perfect atomic structure has been determined utilization anticoagulant stabilization and VKOR-like [https://pubmed.ncbi.nlm.nih.gov/33154105/ homologs]. | ||
