Abstract
Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, binds an iron-responsive element (IRE) present in the 5'untranslated region of the mRNA for erythroid 5-aminolevulinate synthase, the first enzyme of the heme biosynthetic pathway. This IRE-binding activity of ferrochelatase may play a critical role in the regulation of heme biosynthesis in differentiating erythrocytes.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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5-Aminolevulinate Synthetase / biosynthesis*
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Animals
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Binding Sites
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Deoxyribonucleases, Type II Site-Specific
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Erythrocytes / enzymology*
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Ferrochelatase / isolation & purification
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Ferrochelatase / metabolism*
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Iron / metabolism
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Isoenzymes / biosynthesis
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Mice
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RNA, Messenger / metabolism*
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism*
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Restriction Mapping
Substances
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Isoenzymes
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RNA, Messenger
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Recombinant Proteins
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Iron
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5-Aminolevulinate Synthetase
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Deoxyribonucleases, Type II Site-Specific
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GCGGCCGC-specific type II deoxyribonucleases
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GTCGAC-specific type II deoxyribonucleases
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Ferrochelatase