cd00717

URO-D

CDD entry
Member databaseCDD
CDD typedomain
Short nameURO-D
SetURO-D_CIMS_like

Description

Uroporphyrinogen decarboxylase (URO-D) is a dimeric cytosolic enzyme that decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, without requiring any prosthetic groups or cofactors. This reaction is located at the branching point of the tetrapyrrole biosynthetic pathway, leading to the biosynthesis of heme, chlorophyll or bacteriochlorophyll. URO-D deficiency is responsible for the human genetic diseases familial porphyria cutanea tarda (fPCT) and hepatoerythropoietic porphyria (HEP).
[3, 6, 4, 5, 1, 2, 7]

References

1.Crystal structure of human uroporphyrinogen decarboxylase. Whitby FG, Phillips JD, Kushner JP, Hill CP. EMBO J. 17, 2463-71, (1998). View articlePMID: 9564029

2.Porphyria cutanea tarda. Elder GH. Semin. Liver Dis. 18, 67-75, (1998). PMID: 9516680

3.Iron overload in porphyria cutanea tarda. Sampietro M, Fiorelli G, Fargion S. Haematologica 84, 248-53, (1999). PMID: 10189391

4.Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism. Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A. J. Biol. Chem. 276, 44108-16, (2001). View articlePMID: 11524417

5.Novel insights in the control of tetrapyrrole metabolism of higher plants. Grimm B. Curr. Opin. Plant Biol. 1, 245-50, (1998). View articlePMID: 10066589

6.Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase. Phillips JD, Whitby FG, Kushner JP, Hill CP. EMBO J. 22, 6225-33, (2003). View articlePMID: 14633982

7.Uroporphyrinogen decarboxylase. Elder GH, Roberts AG. J. Bioenerg. Biomembr. 27, 207-14, (1995). View articlePMID: 7592567

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