Sandbox Reserved 1716: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 33: | Line 33: | ||
As mentioned above, Vitamin K epoxide is a part of the Vitamin K cycle and required for blood coagulation. In the cycle, VKOR reduces Vitamin K epoxide to Vitamin K Quinone, or the active form of Vitamin K. In this conversion, VKOR donates electrons to Vitamin K epoxide from the S-H of the active pair of cysteines, C132-C135. The mediated cysteine pair, C43-C51, has to be reduced for the transfer of electrons to the substrate to occur. | As mentioned above, Vitamin K epoxide is a part of the Vitamin K cycle and required for blood coagulation. In the cycle, VKOR reduces Vitamin K epoxide to Vitamin K Quinone, or the active form of Vitamin K. In this conversion, VKOR donates electrons to Vitamin K epoxide from the S-H of the active pair of cysteines, C132-C135. The mediated cysteine pair, C43-C51, has to be reduced for the transfer of electrons to the substrate to occur. | ||
Two other notable structures are Vitamin K Quinone (Fig. | Two other notable structures are Vitamin K Quinone (Fig. 4) and Vitamin K Hydroquinone (Fig. 5). Vitamin K Quinone is the product that is released after the reaction with Vitamin K Epoxide and VKOR. (Fig. 1) | ||
[[Image:Vitaminkquinone.PNG|150 px|left|thumb|Figure 4. Vitamin K Quinone structure]] [[Image:Vitaminkhydroquinone.PNG|150 px|right|thumb|Figure 5. Vitamin K Hydroquinone structure]] | [[Image:Vitaminkquinone.PNG|150 px|left|thumb|Figure 4. Vitamin K Quinone structure]] [[Image:Vitaminkhydroquinone.PNG|150 px|right|thumb|Figure 5. Vitamin K Hydroquinone structure]] | ||
