22.214.171.124 - Uroporphyrinogen decarboxylase
- Uroporphyrinogen III decarboxylase.
- Uroporphyrinogen-III carboxy-lyase.
4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
There are no Cofactors for this Enzyme
Uroporphyrinogen decarboxylase (HemE) catalyses the fifth step in heme biosynthesis by converting uroporphyrinogen III to coproporphyrinogen III by decarboxylating the four acetate side chains of the substrate.
The first step in the proposed mechanism is a proton transfer from an acid (Arg37) to the C2 centre of ring D. Computational studies suggest that this first step is rate limiting. The next step is the decarboxylation of the acetate moiety. The final catalytic step in the overall mechanism is regeneration of the protonated Arg37 residue by transfer of a proton from the substrate's --C2H2-- group to its neutral guanidino group with concurrent proton transfer from the guanidinium group of Arg50 to the C3′ centre of the substrate.
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
- Kinetic Parameters
Organism Temperature Range Comment Rattus norvegicus 0 - 70 activity increases with temperature up to 47°C, decreases at 53°C Neohelice granulata 0 - 70 activity increases with temperature up to 47°C, decreases at 53°C
Organism pH Range Comment Homo sapiens 5 - 8 in 0.2 M KH2PO4, 0.1 mM dithiothreitol Oryctolagus cuniculus 5.3 - 8 pH 5.3: about 60% of maximal activity, pH 8.0: about 65% of maximal activity Rattus norvegicus 6 - 8 Gallus gallus 6 - 7.4 pH 6.0: about 55% of maximal activity, pH 7.4: about 50% of maximal activity, uroporphyrinogen III Cereibacter sphaeroides 6.2 - 7.7 pH 6.2: about 25% of maximal activity, pH 7.7: about 70% of maximal activity
- A porphodimethene chemical inhibitor of uroporphyrinogen decarboxylase.
- Re: Porphyria Cutanea Tarda in a Patient with Myelofibrosis.
- Targeting uroporphyrinogen decarboxylase for head and neck cancer treatment
- Hepatoerythropoietic Porphyria Caused by a Novel Homoallelic Mutation in Uroporphyrinogen Decarboxylase Gene in Egyptian Patients.
- A Case Report of Porphyria Cutanea Tarda with Hepatitis-C Virus Co-infection.
- Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.
- Development and validation of metabolic models for predicting survival and immune status of hepatocellular carcinoma patients.
- Improved biosynthesis of heme in Bacillus subtilis through metabolic engineering assisted fed-batch fermentation.
- Uroporphyrinogen decarboxylase: optimizing radiotherapy for head and neck cancer.
- Thiol redox sensitivity of two key enzymes of heme biosynthesis and pentose phosphate pathways: uroporphyrinogen decarboxylase and transketolase.
- Applications of the Whole-Cell System in the Efficient Biosynthesis of Heme.