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9.4B: Selenoproteins

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    As mentioned earlier, selenium's antioxidant function is not due to the mineral itself, but a result of selenoproteins. This is illustrated in the figure below, where the different colored circles represent amino acids in the crescent shaped enzyme. In most enzymes, the mineral is a cofactor that is external to the enzyme, as shown on the left. Selenoenzymes contain selenocysteine as an amino acid in the active site of the enzyme. Thus, in selenoenzymes, selenium does not serve as a cofactor, which is different than most minerals required for enzyme function.

    Figure 9.411.png

    Figure 9.411: Enzyme with a mineral cofactor versus a selenoenzyme

    25 human selenoproteins, containing the amino acid selenocysteine, have been identified. The following table lists these selenoproteins along with their function.

    Table 9.411: The 25 Human Selenoproteins1-3
    Selenoprotein Function
    Glutathione peroxidase 1 (GPX1) Antioxidant enzyme
    Glutathione peroxidase 2 (GPX2) Antioxidant enzyme
    Glutathione peroxidase 3 (GPX3) Antioxidant enzyme
    Glutathione peroxidase 4 (GPX4) Antioxidant enzyme
    Glutathione peroxidase 6 (GPX6) Antioxidant enzyme
    Iodothyronine 5'-deiodinase-1 (DI1) Plasma T3 production
    Iodothyronine 5'-deiodinase-2 (DI2) Local T3 production
    Iodothyronine 5'-deiodinase-3 (DI3) T3 degradation
    Thioredoxin reductase (TR1) Antioxidant enzyme
    Thioredoxin reductase (TR2) Antioxidant enzyme
    Thioredoxin reductase (TR3) Antioxidant enzyme
    Selenophosphate synthetase 2 (SPS2) Selenophosphate synthesis
    Selenoprotein 15 (Sep15) Unknown
    Selenoprotein H (SepH) Unknown
    Selenoprotein I (SepI) Unknown
    Selenoprotein K (SepK) Unknown
    Selenoprotein M (SepM) Unknown
    Selenoprotein N (SepN) Unknown
    Selenoprotein O (SepO) Unknown
    Selenoprotein P (SepP) Unknown
    Selenoprotein R (SepR) Unknown
    Selenoprotein S (SepS) Unknown
    Selenoprotein T (SepT) Unknown
    Selenoprotein V (SepV) Unknown
    Selenoprotein W (SepW) Unknown

    Hopefully from looking at the table, you see that the glutathione peroxidase enzymes and thioredoxin reductases are antioxidant enzymes. The iodothyronine 5'-deiodinases are involved in the metabolism of thyroid hormones, which will be discussed further in the iodine section. For the vast majority of the other selenoproteins, their function isn't known, so they were named selenoprotein and given a letter. As described earlier and shown below, glutathione peroxidase converts hydrogen peroxide into water.

    Figure 9.412.png

    Figure 9.412: Antioxidant enzymes that use minerals as cofactors

    Remember that thioredoxin reductase can regenerate ascorbate from dehydroascorbate in the theorized antioxidant network (shown below).

    Figure 9.413.png

    Figure 9.413 The theorized antioxidant network4


    1. Gladyshev V, Kryukov G, Fomenko D, Hatfield D. (2004) Identification of trace element-containing proteins in genomic databases. Annu Rev Nutr 24: 579-596.
    2. Beckett G, Arthur J. (2005) Selenium and endocrine systems. J Endocrinol 184(3): 455-465.
    3. Stipanuk MH. (2006) Biochemical, physiological, & molecular aspects of human nutrition. St. Louis, MO: Saunders Elsevier.
    4. Packer L, Weber SU, Rimbach G. (2001) Molecular aspects of alpha-tocotrienol antioxidant action and cell signalling. J Nutr 131(2): 369S-373S.

    This page titled 9.4B: Selenoproteins is shared under a CC BY-NC-SA 4.0 license and was authored, remixed, and/or curated by Brian Lindshield via source content that was edited to the style and standards of the LibreTexts platform; a detailed edit history is available upon request.

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