Chemistry:Coproporphyrinogen III
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| IUPAC name
3-[8,12,17-tris(2-carboxyethyl)-3,7,13,18-tetramethyl-5,10,15,20,21,22, 23,24-octahydroporphyrin-2-yl]propanoic acid
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| Identifiers | |
3D model (JSmol)
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| ChemSpider | |
| MeSH | Coproporphyrinogen+III |
PubChem CID
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| Properties | |
| C36H44N4O8 protonated carboxylic acids | |
| Molar mass | 660.757 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
| Infobox references | |
Coproporphyrinogen III is a metabolic intermediate in the biosynthesis of many compounds that are critical for living organisms, such as hemoglobin and chlorophyll. It is a colorless solid.
The compound is a porphyrinogen, a class of compounds characterized by a hexahydroporphine core with various side chains. The coproporphyrinogens have the outermost hydrogen atoms of the core replaced by four methyl groups –CH
3 (M) and four propionic acid groups –CH
2–CH
2–COOH (P). In coproporphyrogen III, the order around the outer ring is MP-MP-MP-PM. For comparison, coproporphyrinogen I has them in the sequence MP-MP-MP-MP. heme.
Biosynthesis and metabolism
In the main porphyrin biosynthesis pathway, coproporphyrinogen III is derived from uroporphyrinogen III by the action of the enzyme uroporphyrinogen III decarboxylase:[1]
The conversion entails four decarboxylations, which turn the four acetic acid groups –CH
2–COOH into methyl groups –CH
3, with release of four carbon dioxide molecules.[2][3]
Coproporphyrinogen III is further used as a substrate for the enzyme coproporphyrinogen III oxidase which oxidizes and further decarboxylates it to protoporphyrinogen IX.[4]
References
- ↑ "Uroporphyrinogen decarboxylation as a benchmark for the catalytic proficiency of enzymes". Proc. Natl. Acad. Sci. U.S.A. 105 (45): 17328–33. November 2008. doi:10.1073/pnas.0809838105. PMID 18988736. Bibcode: 2008PNAS..10517328L.
- ↑ Paul R. Ortiz de Montellano (2008). Wiley Encyclopedia of Chemical Biology. John Wiley & Sons. doi:10.1002/9780470048672.wecb221. ISBN 978-0470048672.
- ↑ Sassa, S.; Kappas, A. (2000). "Molecular aspects of the inherited porphyrias". Journal of Internal Medicine 247 (2): 169–78. doi:10.1046/j.1365-2796.2000.00618.x. PMID 10692079.
- ↑ Enzyme 1.3.3.3 at KEGG Pathway Database.
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