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1. www.ncbi.nlm.nih.gov › pmc › articlesHeme biosynthesis and the porphyrias - PMC

   www.ncbi.nlm.nih.gov › pmc › articles

   The final step of heme biosynthesis is the insertion of iron into protoporphyrin IX (OMIM 612386). This reaction is catalyzed by the mitochondrial enzyme ferrochelatase (see Fig. 1). Ferrochelatase utilizes protoporphyrin IX, rather than its reduced form, as substrate, but requires the reduced ferrous form of iron .

   • Fig. 1

     Porphyrias, is a general term for a group of metabolic...

   • Table 1

     Porphyrias, is a general term for a group of metabolic...

2. www.ncbi.nlm.nih.gov › books › NBK537329Biochemistry, Heme Synthesis - StatPearls - NCBI Bookshelf

   www.ncbi.nlm.nih.gov › books › NBK537329

   May 1, 2023 · The correct porphyrin ring III forms, and then the side chains of uroporphyrinogen III are modified, catalyzed by uroporphyrinogen decarboxylase to produce coproporphyrinogen III. Following its synthesis, coproporphyrinogen III gets transported into mitochondria.

   • Author: Aminat S. Ogun, Neena V. Joy, Menogh Valentine
   • Published: 2023/05/01

   • Publish Year: 2021

3. People also ask

   How is coproporphyrin decarboxylated to heme?

   • Then, coproporphyrin ferrochelatase (CpfC) catalyzes the insertion of Fe 2+ into coproporphyrin III to produce Fe-coproheme III. Finally, coproheme is decarboxylated to heme by coproheme decarboxylase (ChdC). In C. glutamicum, UroD, CgoX, CpfC, and ChdC are encoded by hemE, hemY, hemH, and hemQ, respectively.

   Recent advances in microbial synthesis of free heme | Applied

   link.springer.com/article/10.1007/s00253-023-12968-5

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   What enzyme is involved in heme biosynthesis?

   • Fech is the final enzyme in heme biosynthesis, and it catalyzes the insertion of iron into the protoporphyrin ring to generate heme ( Figure 1 ). Enzyme activity is reduced to 10%–35% of normal in all tissues, though the excess protoporphyrin is mainly produced in bone marrow. 3.7.2.2. Clinical Features

   Clinically Important Features of Porphyrin and Heme Metabolism and the

   www.ncbi.nlm.nih.gov/pmc/articles/PMC4279155/

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   Is heme a ferrous protoporphyrin?

   • Heme is a term used for ferrous protoporphyrin IX (PPIX) that is easily oxidized in vitro to hemin, termed- ferric PPIX. In heme the ferrous iron atom (Fe 2+) has 6 electron pairs, 4 are bound to the pyrrolic nitrogens of the porphyrin macrocyle, leaving two unoccupied electron pairs, one above and the other below the plane of the porphyrin ring.

   Heme biosynthesis and the porphyrias - PMC - National Center for

   www.ncbi.nlm.nih.gov/pmc/articles/PMC7252266/

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   Which enzymatic steps lead to the biosynthesis of protoporphyrin IX (Proto)?

   • In photosynthetic organisms, several enzymatic steps of TBS lead to the biosynthesis of protoporphyrin IX (Proto), which is a common substrate for ferrochelatase (FeCh) and Mg-chelatase (MgCh), two enzymes at the TBS branching point, dedicated to biosynthesis of heme and chlorophyll, respectively.

   The function of PROTOPORPHYRINOGEN IX OXIDASE in chlorophyll ... …

   www.nature.com/articles/s42003-019-0395-5

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4. www.ncbi.nlm.nih.gov › pmc › articlesClinically Important Features of Porphyrin and Heme ...

   www.ncbi.nlm.nih.gov › pmc › articles

   Nov 3, 2014 · Under conditions of iron deficiency, lead poisoning or excessive formation of PP, zinc protoporphyrin (ZnPP) is formed as a by-product in the heme biosynthesis pathway, resulting from insertion of Zn 2+ rather than Fe 2+ into protoporphyrin by FECH. FECH is also capable of inserting cobalt into PP with the formation of cobalt protoporphyrin ...

   • Author: Siddesh Besur, Weihong Hou, Paul Schmeltzer, Herbert L. Bonkovsky
   • DOI: 10.3390/metabo4040977

   • Publish Year: 2014
   • Publication: Metabolites. 2014 Dec; 4(4): 977-1006.

5. link.springer.com › article › 10Recent advances in microbial synthesis of free heme

   link.springer.com › article › 10

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   Jan 9, 2024 · Then, coproporphyrin ferrochelatase (CpfC) catalyzes the insertion of Fe 2+ into coproporphyrin III to produce Fe-coproheme III. Finally, coproheme is decarboxylated to heme by coproheme decarboxylase (ChdC). In C. glutamicum, UroD, CgoX, CpfC, and ChdC are encoded by hemE, hemY, hemH, and hemQ, respectively.

6. www.frontiersin.org › journals › microbiologyFrontiers | Regulation of heme biosynthesis via the ...

   www.frontiersin.org › journals › microbiology

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   Mar 20, 2024 · In some monoderm bacteria, the terminal heme biosynthesis enzyme coproheme decarboxylase (ChdC) and other enzymes of the CPD are found, but the CPD does not appear to be the predominant heme biosynthesis pathway across these phyla.

7. www.nature.com › articles › s42003/019/0395-5The function of PROTOPORPHYRINOGEN IX OXIDASE in ... - Nature

   www.nature.com › articles › s42003/019/0395-5

   May 3, 2019 · In eukaryotic organisms PPOX belongs to the FAD-containing HemY-type protein family 2 and in plants it is encoded by two nucleus-localised homologous genes, PPOX1 and PPOX2. PPOX1 is targeted...

8. www.nature.com › articles › 7310086Heme: a versatile signaling molecule controlling the ... - Nature

   www.nature.com › articles › 7310086

   Aug 8, 2006 · Heme (iron protoporphyrin IX) is an essential molecule for numerous living organisms. Not only does it serve as a prosthetic group in enzymes, it also acts as a signaling molecule that controls...