Sandbox WWC11: Difference between revisions
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''Figure 1. Depicts key amino acids in stabilization of heme in myeloperoxidase.'' <ref name="Myeloperoxidase">PMID:26884610</ref> | ''Figure 1. Depicts key amino acids in stabilization of heme in myeloperoxidase.'' <ref name="Myeloperoxidase">PMID:26884610</ref> | ||
Myeloperoxidase is synthesized in bone marrow along with most other white blood cell components. The myloperoxidase enzyme is composed of two identical subunits. After translation of these subunits, they are cleaved into two parts: the heavy chain and the light chain. The heavy chain is a glycosylated domain that weighs approximately 58.5 kDa. This portion of the enzyme has the deep pocket where the heme is inserted by chaperones (calreticulin and calnexin). <ref name="Neutrophil">PMID:26904693</ref> Click on the green link to see the <scene name='69/696303/Heme_pocket_mpo/1'> | Myeloperoxidase is synthesized in bone marrow along with most other white blood cell components. The myloperoxidase enzyme is composed of two identical subunits. After translation of these subunits, they are cleaved into two parts: the heavy chain and the light chain. The heavy chain is a glycosylated domain that weighs approximately 58.5 kDa. This portion of the enzyme has the deep pocket where the heme is inserted by chaperones (calreticulin and calnexin). <ref name="Neutrophil">PMID:26904693</ref> Click on the green link to see the <scene name='69/696303/Heme_pocket_mpo/1'>MPO heme pocket</scene> in the structure above. The amino acid make up of heme pocket can be seen in Figure 1 above. The pink in this picture is the light chain, the blue is the heavy chain. The light chain (about 13.5 kDa) is attached to the heavy chain through disufide bonds. There have been discoveries of slight variation in the primary sequence of myeloperoxidase. However, for the most part these slight variations do not affect the enzymatic activity. Currently three isoforms have been isolated.<ref name="Enzymatic Activity">PMID:120019</ref> | ||
