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Literature summary for 4.1.1.37 extracted from

  • Mukerji, S.K.; Pimstone, N.R.
    Reduced substrate affinity for human erythrocyte uroporphyrinogen decarboxylase constitutes the inherent biochemical defect in porphyria cutanea tarda (1985), Biochem. Biophys. Res. Commun., 127, 517-525.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00057
-
5-COOH-porphyrinogen I enzyme from healthy individuals Homo sapiens
0.001
-
5-COOH-porphyrinogen I enzyme from patients with sporadic porphyria cutanea tarda Homo sapiens
0.00133
-
Uroporphyrinogen I enzyme from healthy individuals Homo sapiens
0.00215
-
5-COOH-porphyrinogen I enzyme from patients with familial porphyria cutanea tarda Homo sapiens
0.00256
-
Uroporphyrinogen I enzyme from patients with sporadic porphyria cutanea tarda Homo sapiens
0.00533
-
Uroporphyrinogen I enzyme from patients with familial porphyria cutanea tarda Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the familial porphyria cutanea tarda is a genetically determined kinetic abnormality of uroporphyrinogen decarboxylase ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-COOH-porphyrinogen I
-
Homo sapiens Coproporphyrinogen I + CO2
-
?
additional information the familial porphyria cutanea tarda is a genetically determined kinetic abnormality of uroporphyrinogen decarboxylase Homo sapiens ?
-
?
uroporphyrinogen I
-
Homo sapiens coproporphyrinogen I + 4 CO2
-
?