ISSN:
1573-6881
Keywords:
Uroporphyrinogen decarboxylase
;
porphyria
;
iron
;
heme biosynthesis
;
uroporphyrinogen
;
cytochromc P450IA
;
hepatoerythropoietic porphyria
;
porphyria cutanea tarda
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract Uroporphyrinogen decarboxylase (EC 4.1.1.37) catalyzes the decarboxylation of uroporphyrinogen III to coproporphyrinogen III. The amino acid sequences, kinetic properties, and physicochemical characteristics of enzymes from different sources (mammals, yeast, bacteria) are similar, but little is known about the structure/function relationships of uroporphyrinogen decarboxylases. Halogenated and other aromatic hydrocarbons cause hepatic uroporphyria by decreasing hepatic uroporphyrinogen decarboxylase activity. Two related human porphyrias, porphyria cutanea tarda and hepatoerythropoietic porphyria, also result from deficiency of this enzyme. The roles of inherited and acquired factors, including iron, in the pathogenesis of human and experimental uroporphyrias are reviewed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02110035
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