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- W1501715468 abstract "Publisher Summary The regulation of heme biosynthesis in animals has been a topic of interest for many years. It is generally agreed that the first enzyme of the heme pathway, 5-aminolevulinate synthase, determines the rate of heme biosynthesis and the regulation of this enzyme is, therefore, a major focus of this chapter. The heme biosynthetic pathway is present in all cell types except mature erythrocytes. The final step of heme biosynthesis occurs in mitochondria and the heme is then utilized for the formation of different hemoproteins located in mitochondria, microsomes, peroxisomes, the cytosol, and probably the nucleus. Heme can control the biosynthesis of some proteins. In erythroid cells, heme controls the translation of proteins, notably α- and β-globin chains, by modulating the activity of a specific kinase. All nucleated animal cells must synthesize heme for incorporation into respiratory cytochromes, but erythroid and liver cells have the highest rates of heme synthesis. Erythroid cells synthesize about 90% of the total heme in the body for assembly into hemoglobin. Although the bulk of heme in the liver is made in situ , the liver may also obtain some heme from serum haptoglobin–hemoglobin and heme–hemopexin complexes, following intravascular hemolysis. All enzymes of the heme biosynthetic pathway, except for protoporphyrinogen oxidase, have been cloned from higher vertebrates. The genes encoding these enzymes are located on different chromosomes." @default.
- W1501715468 created "2016-06-24" @default.
- W1501715468 creator A5005570513 @default.
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- W1501715468 date "1995-01-01" @default.
- W1501715468 modified "2023-10-06" @default.
- W1501715468 title "Molecular Regulation of Heme Biosynthesis in Higher Vertebrates" @default.
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