Notes in ✧ Heme Synthesis

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Published	01/14/2024	In the first step of heme synthesis, {{c1::glycine}} and {{c2::succinyl-CoA}} are combined to form {{c3::δ-aminolevulinic acid}} via the enzyme {{c4::…
Published	01/14/2024	What is the rate-limiting enzyme of heme synthesis? {{c1::δ-aminolevulinic acid synthase (ALAS)}}
Published	01/14/2024	δ-aminolevulinic acid synthase is regulated via negative feedback by {{c1::glucose}} and {{c2::heme}}
Published	01/14/2024	Does heme synthesis occur in the cytoplasm or mitochondria? {{c1::Both :)}}
Published	01/14/2024	δ-aminolevulinic acid is converted to {{c1::porphobilinogen}} via the enzyme {{c2::δ-aminolevulinic acid dehydratase}} (heme synthesis)
Published	01/14/2024	Porphobilinogen is converted to {{c1::hydroxymethylbilane}} via the enzyme {{c2::porphobilinogen deaminase}} (heme synthesis)
Published	01/14/2024	Hydroxymethylbilane is converted to {{c1::uroporphyrinogen III}} via the enzyme uroporphyrinogen III synthase (heme synthesis)
Published	01/14/2024	Uroporphyrinogen III is converted to {{c1::coproporphyrinogen III}} via the enzyme {{c2::uroporphyrinogen decarboxylase}} (heme synthesis)
Published	01/14/2024	Coproporphyrinogen III is converted to {{c1::protoporphyrin}} (heme synthesis)
Published	01/14/2024	{{c1::Protoporphyrin}} and {{c2::Fe2+}} combine to form {{c3::heme}} via the enzyme {{c4::ferrochelatase}}
Published	01/14/2024	Lead (Pb) poisoning leads to inhibition of the enzymes {{c1::δ-aminolevulinic acid dehydratase}} and {{c2::ferrochelatase}} (heme synthesis)
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