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Literature summary for 4.1.1.37 extracted from

  • Chaufan, G.; Corvi, M.M.; San Martin de Viale, L.C.; Cardenas, M.L.; Rios de Molina Mdel, C.
    Abnormal kinetic behavior of uroporphyrinogen decarboxylase obtained from rats with hexachlorobenzene-induced porphyria (2005), J. Biochem. Mol. Toxicol., 19, 19-24.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Uroporphyrinogen III Rattus norvegicus the enzyme functions in the heme biosynthetic pathway, catalyzing the decarboxylation of the four acetate groups of uroporphyrinogen to form coproporphyrinogen Coproporphyrinogen III + 4 CO2
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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 normal animals and animals with hexachlorobenzene-induced porphyria
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Purification (Commentary)

Purification (Comment) Organism
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 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
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 Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Uroporphyrinogen III the enzyme functions in the heme biosynthetic pathway, catalyzing the decarboxylation of the four acetate groups of uroporphyrinogen to form coproporphyrinogen Rattus norvegicus Coproporphyrinogen III + 4 CO2
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 ?
Uroporphyrinogen III with the enzyme from normal animals, uroporphyrinogen and pentacarboxy-porphyrinogen react at the same active site, i.e. the first and fourth decarboxylation occur at the same site. In animals with hexachlorobenzene-induced porphyria the two reactions occur at functionally different sites, but with cross-inhibition. This suggests that hexachlorobenzene causes the two active sites to become nonequivalent and functionally different Rattus norvegicus Coproporphyrinogen III + 4 CO2
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