Sandbox WWC11: Difference between revisions
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Myeloperoxidase (MPO) is a protein found in nertrophil, the most common white blood cell. This enzyme generates hypochlorous acid (HOCl) from hydrogen peroxide in addition to other hypohalous acids depending on what is available in the cell. The HOCl is then used, in combination with other molecules, in an oxidative burst that kills bacteria and other potentially harmful invaders one taken up by the cell. This protein falls into a group of heme peroxidase enzymes. The role of these enzymes is to oxidize molecules using the heme<ref name="Hampton">PMID:9787133</ref>. <ref name="Takata">PMID:15242101</ref> | Myeloperoxidase (MPO) is a protein found in nertrophil, the most common white blood cell. This enzyme generates hypochlorous acid (HOCl) from hydrogen peroxide in addition to other hypohalous acids depending on what is available in the cell. The HOCl is then used, in combination with other molecules, in an oxidative burst that kills bacteria and other potentially harmful invaders one taken up by the cell. This protein falls into a group of heme peroxidase enzymes. The role of these enzymes is to oxidize molecules using the heme<ref name="Hampton">PMID:9787133</ref>. <ref name="Takata">PMID:15242101</ref> <ref group="xtra">PMID:15068885</ref> | ||
This protein is composed of two identical monomers linked by a cystine bridge. The total molecular weight of this protein is 146kDa. These two monomers can work independently to each other and consist of a light and heavy amino acid chain. The active site on the protein consists of a deep crevice where a heme molecule is covalently attached. The deep pocket is believe to limit access to the heme and increase specificity for smaller molecules to be oxidized. This pocket also possesses a hydrophobic pocket for stabilization of substrate.<ref name="Active Site Structure">PMID:16288920</ref> | This protein is composed of two identical monomers linked by a cystine bridge. The total molecular weight of this protein is 146kDa. These two monomers can work independently to each other and consist of a light and heavy amino acid chain. The active site on the protein consists of a deep crevice where a heme molecule is covalently attached. The deep pocket is believe to limit access to the heme and increase specificity for smaller molecules to be oxidized. This pocket also possesses a hydrophobic pocket for stabilization of substrate.<ref name="Active Site Structure">PMID:16288920</ref> | ||