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Information on EC 4.1.1.37 - uroporphyrinogen decarboxylase
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4.1.1.37 uroporphyrinogen decarboxylaseIUBMB Comments
Acts on a number of porphyrinogens.
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Word Map
- 4.1.1.37
- porphyria
-
cutanea
- tarda
- heme
- erythrocyte
-
porphyrinogenic
- hexachlorobenzene
- urinary
-
hepatoerythropoietic
- porphobilinogen
- overload
-
photosensitivity
-
ferrochelatase
- protoporphyrin
- hemochromatosis
-
5-aminolaevulinate
-
heptacarboxylic
-
hexachlorobenzene-induced
- hypertrichosis
-
phlebotomy
-
erythropoietic
-
delta-aminolaevulinic
-
polyhalogenated
-
5-aminolevulinic
- protoporphyrinogen
-
uroporphyria
- tetrapyrrole
-
sun-exposed
- blister
- siderosis
- diagnostics
-
3,4,3\',4\'-tetrachlorobiphenyl
- medicine
-
hcb-induced
-
miliae
- coproporphyria
- bulla
- agriculture
-
hepta
The enzyme appears in viruses and cellular organisms
Synonyms
uroporphyrinogen decarboxylase, uro-d, porphyrinogen carboxy-lyase, uroporphyrinogen iii decarboxylase, urod protein, uroporphyrinogen-decarboxylase, uro-decarboxylase, uroporphyrinogen-iii decarboxylase, hem12p, tobacco urod, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, uroporphyrinogen
-
-
-
-
Porphyrinogen carboxy-lyase
rl-UroD
UPD
-
-
-
-
URO-D
UroD
uroporphyrinogen decarboxylase
Uroporphyrinogen III decarboxylase
-
-
-
-
uroporphyrinogen-III decarboxylase
Porphyrinogen carboxy-lyase
-
-
-
-
URO-D
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
uroporphyrinogen III = coproporphyrinogen III + 4 CO2
mechanism and stereochemistry
-
uroporphyrinogen III = coproporphyrinogen III + 4 CO2
the decarboxylation of uroporphyrinogen occurs in two stages, via 7 COOH and then 6 and 5 COOH intermediates, with the decarboxylation of the 7 COOH compound being the rate-limiting step for the reaction
-
uroporphyrinogen III = coproporphyrinogen III + 4 CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
uroporphyrinogen-III carboxy-lyase (coproporphyrinogen-III-forming)
Acts on a number of porphyrinogens.
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CAS REGISTRY NUMBER
COMMENTARY
9024-70-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
heptaporphyrinogen III
hexaporphyrinogen III + CO2
-
formation of the stepwise decarboxylation products, hepta-, hexa-, penta-, and coproporphyrinogen III
-
-
?
hexaporphyrinogen III
pentaporphyrinogen III + CO2
-
formation of the stepwise decarboxylation products, hepta-, hexa-, penta-, and coproporphyrinogen III
-
-
?
uroporphyrinogen III
heptaporphyrinogen III + CO2
-
formation of the stepwise decarboxylation products, hepta-, hexa-, penta-, and coproporphyrinogen III
-
-
?
8-carboxylporphyrinogen
coproporphyrinogen(4-COOH) + CO2
-
-
-
?
uroporphyrinogen I
coproporphyrinogen I + 4 CO2
-
-
-
-
?
uroporphyrinogen I
coproporphyrinogen I + 4 CO2
-
formation of the stepwise decarboxylation products, hepta-, hexa-, penta-, and coproporphyrinogen I
-
-
?
uroporphyrinogen I
coproporphyrinogen I + 4 CO2
-
at 50% of the activity with uroporphyrinogen III
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
-
-
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the heme biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth step in heme biosynthetic pathway, four sequential decarboxylation reactions
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
tetrapyrrole coordination, fifth step in the heme biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the heme biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
involved in biosynthesis of chlorophyll and haem
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
tetrapyrrole biosynthetic pathway, normally associated with pathogen defense
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the haem biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
heme pathway enzyme, catalyzes the stepwise decarboxylation of porphyrinogen acetic chains
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
the enzyme functions in the heme biosynthetic pathway, catalyzing the decarboxylation of the four acetate groups of uroporphyrinogen to form coproporphyrinogen
-
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
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
-
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the haem biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
the decarboxylation of the 7-COOH porphyrinogen is the rate-limiting step
-
-
?
uroporphyrinogen-III
coproporphyrinogen-III + 4 CO2
use of Pd/C and hydrogen in reducing uroporphyrin to uroporphyrinogen for use as a substrate for uroporphyrinogen decarboxylase activity assay
-
-
?
uroporphyrinogen-III
coproporphyrinogen-III + CO2
-
first branching point of the ubiquitous tetrapyrrole biosynthetic pathway, chlorophyll and heme biosynthesis
-
?
additional information
?
-
-
the enzyme catalyzes the fifth step in the heme biosynthetic pathway
-
-
?
additional information
?
-
-
porphyria cutanea tarda and hepatoerythropoietic porphyria result from deficiency of uroporphyrinogen decarboxylase
-
-
?
additional information
?
-
-
the familial porphyria cutanea tarda is a genetically determined kinetic abnormality of uroporphyrinogen decarboxylase
-
-
?
additional information
?
-
-
the enzyme is involved in biosynthesis of porphyrin
-
-
?
additional information
?
-
-
porphyria cutanea tarda results from a decreased activity of uroporphyrinogen decarboxylase, the fifth enzyme in heme biosynthesis. The frequency of familial porphyria cutanea tarda in Chile is approximately 50%
-
-
?
additional information
?
-
-
loss of the enzyme activity is a key event in both the induction and the persistence of porphyria
-
-
?
additional information
additional information
-
-
-
the pattern of accumulation of intermediate 7-COOH-porphyrinogens, 6-COOH-porphyrinogens and 5-COOH-porphyrinogens and final coproporphyrinogen decarboxylation products is affected by the ratio of substrate concentration of uroporphyrinogen I or II to enzyme concentration. Under physiological conditions, where the uroporphyrinogen to enzyme ratio is low, the substrate is nearly quantitatively decarboxylated, and the major product is coproporphyrinogen
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
uroporphyrinogen-III
coproporphyrinogen-III + CO2
-
first branching point of the ubiquitous tetrapyrrole biosynthetic pathway, chlorophyll and heme biosynthesis
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the heme biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth step in heme biosynthetic pathway, four sequential decarboxylation reactions
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
tetrapyrrole coordination, fifth step in the heme biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the heme biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
involved in biosynthesis of chlorophyll and haem
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
tetrapyrrole biosynthetic pathway, normally associated with pathogen defense
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the haem biosynthetic pathway
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
heme pathway enzyme, catalyzes the stepwise decarboxylation of porphyrinogen acetic chains
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
the enzyme functions in the heme biosynthetic pathway, catalyzing the decarboxylation of the four acetate groups of uroporphyrinogen to form coproporphyrinogen
-
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
-
fifth enzyme of the haem biosynthetic pathway
-
?
additional information
?
-
-
the enzyme catalyzes the fifth step in the heme biosynthetic pathway
-
-
?
additional information
?
-
-
porphyria cutanea tarda and hepatoerythropoietic porphyria result from deficiency of uroporphyrinogen decarboxylase
-
-
?
additional information
?
-
-
the familial porphyria cutanea tarda is a genetically determined kinetic abnormality of uroporphyrinogen decarboxylase
-
-
?
additional information
?
-
-
the enzyme is involved in biosynthesis of porphyrin
-
-
?
additional information
?
-
-
porphyria cutanea tarda results from a decreased activity of uroporphyrinogen decarboxylase, the fifth enzyme in heme biosynthesis. The frequency of familial porphyria cutanea tarda in Chile is approximately 50%
-
-
?
additional information
?
-
-
loss of the enzyme activity is a key event in both the induction and the persistence of porphyria
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme does not require cofactors or prosthetic groups for activity
-
additional information
-
enzyme does not require cofactors or prosthetic groups for activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-COOH-porphyrin III
-
most effective inhibitor of decarboxylation of both uroporphyrinogen III and 7-COOH-porphyrinogen III
Fe2+
-
0.45 mM Fe(NH4)2, 50% inhibition under anaerobic conditions in the dark. Competitive with uroporphyrinogen I and uroporphyrinogen II as substrates. Preincubation with 5-COOH-porphyrinogen protects
Uroporphyrinogen I
-
light-dependent and light-independent inactivation. The velocity of dark inactivation increases with increasing temperature in the range of 0-45 C
uroporphyrinogen III
-
inhibits decarboxylation of uroporphyrinogen I, no inhibition of 7-COOH-series II porphyrinogens and 5-COOH-series II porphyrinogens decarboxylation
additional information
-
the P-448 isoenzyme of cytochrome P-450 plays an obligatory role in the inhibition of the uroporphyrinogen decarboxylase caused by halogenated biphenyls
-
additional information
-
inhibitor derived from a soluble component of the homogenate of a xenobiotic-treated chicken embryo hepatocyte culture
-
additional information
not inhibited by acebutulol, naproxen, verapramil, and furosemide
-
additional information
-
uroporphyrinogen oxidation catalyzed by microsomes from a methylcholanthrene-treated mouse inhibits the uroporphyrinogen decarboxylase activity
-
additional information
-
no inhibition of pentacarboxyporphyrinogen III decarboxylation
-
additional information
-
neither DTT or GSH affects enzyme activity significantly
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
5-COOH-porphyrinogen I
-
enzyme from patients with sporadic porphyria cutanea tarda
0.00215
5-COOH-porphyrinogen I
-
enzyme from patients with familial porphyria cutanea tarda
0.00256
Uroporphyrinogen I
-
enzyme from patients with sporadic porphyria cutanea tarda
0.00533
Uroporphyrinogen I
-
enzyme from patients with familial porphyria cutanea tarda
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
recombinant mutant A22V substrate uroporphyrinogen-I, 62.6% of recombinant wild-type activity
additional information
-
recombinant mutant A22V substrate uroporphyrinogen-I, 62.6% of recombinant wild-type activity
additional information
recombinant mutant A22V substrate uroporphyrinogen-III, 73.2% of recombinant wild-type activity
additional information
-
recombinant mutant A22V substrate uroporphyrinogen-III, 73.2% of recombinant wild-type activity
additional information
recombinant mutant F84I substrate uroporphyrinogen-I, 1.7% of recombinant wild-type activity
additional information
-
recombinant mutant F84I substrate uroporphyrinogen-I, 1.7% of recombinant wild-type activity
additional information
recombinant mutant F84I substrate uroporphyrinogen-III, 2.3% of recombinant wild-type activity
additional information
-
recombinant mutant F84I substrate uroporphyrinogen-III, 2.3% of recombinant wild-type activity
additional information
recombinant mutant T141I substrate uroporphyrinogen-I, 21.3% of recombinant wild-type activity
additional information
-
recombinant mutant T141I substrate uroporphyrinogen-I, 21.3% of recombinant wild-type activity
additional information
recombinant mutant T141I substrate uroporphyrinogen-III, 26.7% of recombinant wild-type activity
additional information
-
recombinant mutant T141I substrate uroporphyrinogen-III, 26.7% of recombinant wild-type activity
additional information
recombinant mutant Y182C substrate uroporphyrinogen-I, 40.0% of recombinant wild-type activity
additional information
-
recombinant mutant Y182C substrate uroporphyrinogen-I, 40.0% of recombinant wild-type activity
additional information
recombinant mutant Y182C substrate uroporphyrinogen-III, 65.2% of recombinant wild-type activity
additional information
-
recombinant mutant Y182C substrate uroporphyrinogen-III, 65.2% of recombinant wild-type activity
additional information
recombinat mutant G318R substrate uroporphyrinogen-I 60.9 percent of recombinant wild-type
additional information
-
recombinat mutant G318R substrate uroporphyrinogen-I 60.9 percent of recombinant wild-type
additional information
recombinat mutant G318R substrate uroporphyrinogen-III 76.2 percent of recombinant wild-type
additional information
-
recombinat mutant G318R substrate uroporphyrinogen-III 76.2 percent of recombinant wild-type
additional information
recombinat mutant K297N substrate uroporphyrinogen-I 63.1 percent of recombinant wild-type
additional information
-
recombinat mutant K297N substrate uroporphyrinogen-I 63.1 percent of recombinant wild-type
additional information
recombinat mutant K297N substrate uroporphyrinogen-III 73.7 percent of recombinant wild-type
additional information
-
recombinat mutant K297N substrate uroporphyrinogen-III 73.7 percent of recombinant wild-type
additional information
subnormal uroporphyrinogen decarboxylase activity results in accumulation and urinary excretion of uroporphyrin and heptacarboxyl porphyrin
additional information
-
subnormal uroporphyrinogen decarboxylase activity results in accumulation and urinary excretion of uroporphyrin and heptacarboxyl porphyrin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
5.7
-
uroporphyrinogen I, uroporphyrinogen III or 7-COOH-porphyrinogen I, estimation by coproporphyrinogen formation
6.2
6.8
7.2
7.6
-
partial reactions: synthesis of 6-COOH porphyrinogen and 5-COOH porphyrinogen from uroporphyrinogen I
7.2
-
coproporphyrinogen formation from uroporphyrinogen I, parzial reactions: synthesis of 4-COOH-porphyrinogen III and 6-COOH-porphyrinogen from uroporphyrinogen III
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.6
-
pH 5.0: about 80% of maximal activity, pH 6.6: about 40% of maximal activity, 5-COOH-porphyrinogen I
5.3 - 8
-
pH 5.3: about 60% of maximal activity, pH 8.0: about 65% of maximal activity
5.8 - 7.4
-
pH 5.8: about 65% of maximal activity, pH 7.4: about 45% of maximal activity, uroporphyrinogen I
5.8 - 7.8
-
pH 5.8: about 60% of maximal activity, pH 7.8: about 55% of maximal activity, 5-COOH-porphyrinogen III
6 - 7.2
-
pH 6.0: about 50% of maximal activity, pH 7.2: about 60% of maximal activity, uroporphyrinogen III
6 - 7.4
-
pH 6.0: about 55% of maximal activity, pH 7.4: about 50% of maximal activity, uroporphyrinogen III
6.2 - 7.7
-
pH 6.2: about 25% of maximal activity, pH 7.7: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 70
0 - 70
-
activity increases with temperature up to 47°C, decreases at 53°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
German backface sheep, mutation L131P is associated with a type pf porphyria
-
-
brenda
-
4420, 4425, 4428, 4430, 4432, 4438, 4440, 4442, 4448, 4449, 4450, 4451, 664858, 682571, 682774, 684418, 691874, 691975, 692689
-
-
brenda
normal animals and animals with hexachlorobenzene-induced porphyria
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
-
hepatoerythropoietic porphyria results from a deficiency of uroporphyrinogen decarboxylase
malfunction
-
UROD knockdown plus radiation induces caspase-mediated apoptosis and cell cycle arrest in head and neck cancer cells in vitro and suppresses the in vivo tumor-forming capacity of head and neck cancer cells, as well as delays the growth of established tumor xenografts in mice
malfunction
humans deficient in UROD present with porphyria cutanea tarda, a condition characterized by light-sensitive dermatitis, excretion of excess uroporphyrins, and associated hepatic porphyrin accumulation
metabolism
uroporphyrinogen decarboxylase, Hem12p, is involved in the 5th step of heme biosynthesis in the cytosol, before biosynthesis is completed within mitochondria
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
41000
41070
42000
44000
-
x * 44000, uroporphyrinogen decarboxylase containing a histidine tag on the amino terminal end, SDS-PAGE
46000
54000
66000
-
uroporphyrinogen decarboxylase containing a histidine tag on the amino terminal end, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
?
-
x * 44000, uroporphyrinogen decarboxylase containing a histidine tag on the amino terminal end, SDS-PAGE
dimer
SDS-PAGE, the dimeric structure of uroporphyrinogen decarboxylase is required to achieve conformational stability and to create a large active-site cleft
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glutathionylation
Cys52 of the enzyme can be glutathionylated and subsequently deglutathionylated by Grx2p in vitro
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion with 25% polyethylene glycol-monomethyl ether 2000 and 160 mM sodium acetate in 100 mM citrate, pH 5.6, at 20°C
-
crystallized in complex with coproporphyrinogen by sitting drop vapor diffusion, crystals belong to space group P3(1)21, unit cell dimensions a : b :102.9 A, c : 74.5 A
modified enzyme single-chain URO-D crystals are isomorphous with wild-type uroporphyrinogen decarboxylase crystals
hanging drop vapor diffusion method, space group P622,unit cell constants a : b : 158.44 A, c : 67.68 A
-
hexagonal space group P622, unit cell parameters a : b : 158.44 A, c : 67.68 A
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A80S
-
less than 12% of the specific activity of wild-type enzyme, Q38R-glutathione S-transferase fusion protein
F217Y
G170D
-
the missense mutation is associated with hepatoerythropoietic porphyria and shows erythrocyte UROD activity of 42% of normal. The recombinant UROD protein shows a relative activity of 17% and 60% of wild type to uroporphyrinogen I and III respectively
G318R
little effect on the structure or activity of recombinant uroporphyrinogen decarboxylase, but the protein displays reduced stability in vitro
K297N
little effect on the structure or activity of recombinant uroporphyrinogen decarboxylase, but the protein displays reduced stability in vitro
M1I
the absence of an initial methionine codon within the messenger RNA (mRNA) Kozac consensus sequence is predicted to lead to a loss of translation from the mutant allele
Q116X
this may yield a truncated protein of 115 amino acids or nonsense-mediated mRNA decay
Q38R
-
less than 0.2% of the specific activity of wild-type enzyme, Q38R-glutathione S-transferase fusion protein
T160I
-
3.4% of the specific activity of wild-type enzyme, Q38R-glutathione S-transferase fusion protein
Y164G
K150T
-
the mutation does not have a significant effect on Vmax, but decreases Km by 25%
K150T/K219E/K277P
-
the mutant shows no significant change in Km, but the Vmax increases by 3.7fold
additional information
F217Y
recombinant mutant of the single chain of both modules substrate uroporphyrinogen-I, 2.5% of recombinant wild-type
F217Y
recombinant mutant of the single chain of both modules substrate uroporphyrinogen-III, 14.5% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the first module substrate uroporphyrinogen-I, 41.3% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the first module substrate uroporphyrinogen-II, 50.9% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the second module substrate uroporphyrinogen-I, 46.2% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the second module substrate uroporphyrinogen-III, 52.7% of recombinant wild-type
F217Y
recombinant mutant substrate uroporphyrinogen-I, 2.6% of recombinant wild-type
Y164G
recombinant mutant of the single chain of the first module substrate uroporphyrinogen-I, 13.2% of recombinant wild-type
Y164G
recombinant mutant substrate uroporphyrinogen-I, 8.1% of recombinant wild-type
additional information
5del10, this may yield a truncated protein of 115 amino acids or nonsense-mediated mRNA decay
additional information
-
5del10, this may yield a truncated protein of 115 amino acids or nonsense-mediated mRNA decay
additional information
construction of a single-chain protein (single-chain URO-D) in which the two subunits are connected by a flexible linker. The crystal structure of this protein is shown to be superimposable with wild-type activity and to have comparable catalytic activity
additional information
variants of the linked dimer in which either of the active sites is inactivated by site-directed mutagenesis maintained approximately half of the wildtype catalytic activity, all four decarboxylations can be catalyzed at a single active site and shuttling of intermediates between active sites of the uroporphyrinogen decarboxylase dimer is not required
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
55
60
65
60
-
20 min, 52% loss of activity of the liver enzyme, 55% loss of activity of the erythrocyte enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
recombinant enzymes are catalytically less efficient compared with the host enzyme
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 4°C, 50 mM sodium phosphate buffer, pH 7.5, containing 300 mM imidazole, 1% Triton X-100, 50 mM NaCl, and 10% glycerol, more than a week, significant loss in activity
-
-20°C, in 30-70% ammonium saturation fraction, 2 weeks, remains stable
-
-20°C, in 30-70% ammonium saturation fraction, 8 weeks, 50% loss of activity
-
frozen in 25 mM potassium phosphate buffer, pH 7.0, containing 2-mercaptoethanol, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
IMAC column chromatography, Mono Q column chromatography, and Superdex 70 gel filtration
-
Ni-NTA column chromatography
substrate ligand column is developed by covalently linking coproporphyrin-III to a Sepharose resin. The ligand-resin chromatography step rapidly separates coproporphyrinogen oxidase from uroporphyrinogen decarboxylase
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
native enzyme and N-terminally truncated UROD are expressed in Escherichia coli Rosetta2(DE3)pLysS cells
-
wild-type enzyme and mutants causing porphyria cutanea tarda, expression in Escherichia coli BL-21
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
diagnostics
-
uroporphyrinogen decarboxylase activity has a high diagnostic accuracy for differentiating the 2 Porphyria cutanea tarda types, the sporadic (sPCT) and familial (fPCT) forms, which are generally clinically indistinguishable, a model that takes into account both clinical information and laboratory test results can be used to predict fPCT
medicine
agriculture
-
first step to establish this enzyme as a possible biomarker for environmental contamination
agriculture
-
first step to establish this enzyme as a possible biomarker for environmental contamination
agriculture
-
first step to establish this enzyme as a possible biomarker for environmental contamination
-
medicine
-
malfunction of UROD is associated with porphyria cutanea tarda and hepatoerythropoietic porphyria, denaturing gradient gel electrophoresis technique DGGE assay presents genetic diagnosis method for screening patients from previously uncharacterized families, differential diagnosis between familial and sporadic cases of PCT
medicine
-
PCT is a human metabolic disorder, due to the acquired or genetic impairment of uroporphyrinogen decarboxylase activity
medicine
subnormal activity of uroporphyrinogen decarboxylase in hepatocytes is responsible for the most common form of porphyria in humans, porphyria cutanea tarda
medicine
-
a low erythrocytic UROD may be a predisposing factor for porphyria cutanea tarda
medicine
-
the clinical manifestations of Porphyria cutanea tarda in dialysis patients can be a result of reduced activity of uroporphyrinogen decarboxylase in addition to the accumulation of photosensitive by-products resulting from a lack of an effective means of excretion
medicine
-
uroporphyrinogen decarboxylase is a radiosensitizing target for head and neck cancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mauzerall, D.; Granick, S.
Porphyrin biosynthesis in erythrocytes. III. Uroporphyrinogen and its decarboxylase
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Oryctolagus cuniculus
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Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
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1970
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Porphyrin biosynthesis. X-Porphyrinogen carboxy-lyase from avian erythrocytes. Further properties
Biochim. Biophys. Acta
309
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1973
Gallus gallus
brenda
De Verneuil, H.; Grandchamp, B.; Nordmann, Y.
Some kinetic properties of human red cell uroporphyrinogen decarboxylase
Biochim. Biophys. Acta
611
174-186
1980
Homo sapiens
brenda
Barnard, G.F.; Akhtar, M.
Stereochemical and mechanistic studies on the decarboxylation of uroporphyrinogen III in haem biosynthesis
J. Chem. Soc. Perkin Trans. I
1979
2354-2363
1979
Gallus gallus
brenda
Smith, A.G.; Francis, J.E.
Decarboxylation of porphyrinogens by rat liver uroporphyrinogen decarboxylase
Biochem. J.
183
455-458
1979
Rattus norvegicus
brenda
Kardish, R.M.; Woods, J.S.
Measurement of heme biosynthetic enzymes in mammalian tissues. I. Uroporphyrinogen decarboxylase
J. Appl. Biochem.
2
159-167
1980
Rattus norvegicus
-
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Investigations of rat liver uroporphyrinogen decarboxylase. Comparisons of porphyrinogens I and III as substrates and the inhibition by porphyrins
Biochem. J.
195
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1981
Rattus norvegicus
brenda
De Verneuil, H.; Sassa, Sh.; Kappas, A.
Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes
J. Biol. Chem.
258
2454-2460
1983
Homo sapiens
brenda
Kawanishi, S.; Seki, Y.; Sano, S.
Uroporphyrinogen decarboxylase. Purification, properties, and inhibition by polychlorinated biphenyl isomers
J. Biol. Chem.
258
4285-4292
1983
Gallus gallus
brenda
Straka, J.G.; Kushner, J.P.
Purification and characterization of bovine hepatic uroporphyrinogen decarboxylase
Biochemistry
22
4664-4672
1983
Bos taurus
brenda
Elder, G.H.; Tovey, J.A.; Sheppard, D.M.
Purification of uroporphyrinogen decarboxylase from human erythrocytes
Biochem. J.
215
45-55
1983
Homo sapiens
brenda
Francis, J.E.; Smith, A.G.
Assay of mouse liver uroporphyrinogen decarboxylase by reverse-phase-performance liquid chromatography
Anal. Biochem.
138
404-410
1984
Mus musculus
brenda
Elder, G.H.; Urquhart, A.J.
Human uroporphyrinogen decarboxylase. Do tissue-specific isoenzymes exist?
Biochem. Soc. Trans.
12
663-664
1984
Homo sapiens
-
brenda
Sinclair, P.R.; Bement, W.J.; Bonkovsky, H.L.; Sinclair, J.F.
Inhibition of uroporphyrinogen decarboxylase by halogenated biphenyls in chick hepatocyte cultures
Biochem. J.
222
737-748
1984
Gallus gallus
brenda
Mukerji, S.K.; Pimstone, N.R.
Reduced substrate affinity for human erythrocyte uroporphyrinogen decarboxylase constitutes the inherent biochemical defect in porphyria cutanea tarda
Biochem. Biophys. Res. Commun.
127
517-525
1985
Homo sapiens
brenda
Mukerji, S.K.; Pimstone, N.R.
In vitro studies of the mechanism of inhibition of rat liver uroporphyrinogen decarboxylase activity by ferrous iron under anaerobic conditions
Arch. Biochem. Biophys.
224
619-629
1986
Rattus norvegicus
brenda
Seki, Y.; Kawanishi, S.; Sano, S.
Uroporphyrinogen decarboxylase purification from chicken erythrocytes
Methods Enzymol.
123
415-421
1986
Gallus gallus
brenda
Koopmann, G.E.; Juknat de Geralnik, A.A.; del C.Batlle, A.M.
Porphyrin biosynthesis in Rhodopseudomonas palustris - V. Purification of porphyrinogen decarboxylase and some unusual properties
Int. J. Biochem.
18
935-944
1986
Rhodopseudomonas palustris
-
brenda
Francis, J.E.; Smith, A.G.
Oxidation of uroporphyrinogens by hydroxyl radicals. Evidence for nonporphyrin products as potential inhibitors of uroporphyrinogen decarboxylase
FEBS Lett.
233
311-314
1988
Mus musculus
brenda
Romana, M.; le Boulch, P.; Romeo, P.H.
Rat uroporphyrinogen decarboxylase cDNA: nucleotide sequence and comparison to human uroporphyrinogen decarboxylase
Nucleic Acids Res.
15
7211
1987
Rattus norvegicus
brenda
Mukerji, S.K.; Pimstone, N.R.
Evidence for two uroporphyrinogen decarboxylase isoenzymes in human erythrocytes
Biochem. Biophys. Res. Commun.
146
1196-1203
1987
Homo sapiens
brenda
Mock, H.P.; Trainotti, L.; Kruse, E.; Grimm, B.
Isolation, sequencing and expression of cDNA sequences encoding uroporphyrinogen decarboxylase from tobacco and barley
Plant Mol. Biol.
28
245-256
1995
Hordeum vulgare, Nicotiana tabacum
brenda
Roberts, A.G.; Elder, G.H.
Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes
Methods Enzymol.
281
349-355
1997
Homo sapiens
brenda
Green-Thompson, R.P.; Kimmett, S.M.; Marks, G.S.
Inhibition of chick embryo hepatic uroporphyrinogen decarboxylase by components of xenobiotic-treated chick embryo hepatocytes in culture. II.
Can. J. Physiol. Pharmacol.
70
939-942
1992
Gallus gallus
brenda
Laterriere, M.; Langlois d'Estaintot, B.; Dautant, A.; Precigoux, G.; Hombrados, I.; de Verneuil, H.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of human uroporphyrinogen decarboxylase
Acta Crystallogr. Sect. D
54
476-478
1998
Homo sapiens
-
brenda
Felix, F.; Brouillet, N.
Purification and properties of uroporphyrinogen decarboxylase from Saccharomyces cerevisiae
Eur. J. Biochem.
188
393-403
1990
Saccharomyces cerevisiae
brenda
Juknat, A.A.; Seubert, A.; Seubert, S.; Ippen, H.
Studies on uroporphyrinogen decarboxylase of etiolated Euglena gracilis Z
Eur. J. Biochem.
179
423-428
1989
Euglena gracilis, Euglena gracilis Z
brenda
Jones, R.M.; Jordan, P.M.
Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides
Biochem. J.
293
703-712
1993
Cereibacter sphaeroides
brenda
Lambrecht, R.W.; Jacobs, J.M.; Sinclair, P.R.; Sinclair, J.F.
Inhibition of uroporphyrinogen decarboxylase activity. The role of cytochrome P-450-mediated uroporphyrinogen oxidation
Biochem. J.
269
437-441
1990
Mus musculus
brenda
Mylchreest, E.; Charbonneau, M.
Studies on the mechanism of uroporphyrinogen decarboxylase inhibition in hexachlorobenzene-induced porphyria in the female rat
Toxicol. Appl. Pharmacol.
145
23-33
1997
Rattus norvegicus
brenda
Afonso, S.G.; Chinarro, S.; de Salamanca, R.E.; del C.Batlle, A.M.
Further evidence on the photodynamic and the novel non-photodynamic inactivation of uroporphyrinogen decarboxylase by uroporphyrin I
J. Enzyme Inhib.
5
225-233
1991
Homo sapiens
brenda
Mukerji, S.K.; Pimstone, N.R.
Uroporphyrinogen decarboxylases from human erythrocytes: purification, complete separation and partial characterization of two isoenzymes
Int. J. Biochem.
24
105-119
1992
Homo sapiens
brenda
Elder, G.H.; Roberts, A.G.
Uroporphyrinogen decarboxylase
J. Bioenerg. Biomembr.
27
207-214
1995
Homo sapiens
brenda
Phillips, J.D.; Whitby, F.G.; Kushner, J.P.; Hill, C.P.
Characterization and crystallization of human uroporphyrinogen decarboxylase
Protein Sci.
6
1343-1346
1997
Homo sapiens
brenda
Mock, H.P; Heller, W.; Molina, A.; Neubohn, B.; Sandermann, H.; Grimm, B.
Expression of uroporphyrinogen decarboxylase or coproporphyrinogen oxidase antisense RNA in tobacco induces pathogen defense responses conferring increased resistance to tobacco mosaic virus
J. Biol. Chem.
274
4231-4238
1999
Nicotiana tabacum
brenda
Martins, B.M.; Grimm, B.; Mock, H.P.; Richter, G.; Huber, R.; Messerschmidt, A.
Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-ray analysis
Acta Crystallogr. Sect. D
57
1709-1711
2001
Nicotiana tabacum
brenda
Billi de Catabbi, S.; Wainstok de Calmanovici, R.; Minutolo, C.; Aldonatti, C.; San Martin de Viale, L.C.
Porphyria-induced hepatic porphyrinogen carboxy-lyase inhibitor and its interaction with the active site(s) of the enzyme
Biochem. Mol. Biol. Int.
47
945-956
1999
Rattus norvegicus
brenda
Phillips, J.D.; Parker, T.L.; Schubert, H.L.; Whitby, F.G.; Hill, C.P.; Kushner, J.P.
Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase
Blood
98
3179-3185
2001
Homo sapiens (P06132), Homo sapiens
brenda
Tavazzi, D.; Di Montemuros, F.M.; Fargion, S.; Fracanzani, A.L.; Fiorelli, G.; Cappellini, M.D.
Levels of uroporphyrinogen decarboxylase (URO-D) in erythrocytes of Italian porphyria cutanea tarda patients
Cell. Mol. Biol.
48
27-32
2002
Homo sapiens
brenda
Chaufan, G.; Corvi, M.; Armesto, A.; San Martin de Viale, L.C.; Luquet, C.; Rios de Molina, M.
Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
Comp. Biochem. Physiol. B
133
251-256
2002
Neohelice granulata, Rattus norvegicus, Rattus norvegicus Wistar
brenda
Phillips, J.D.; Whitby, F.G.; Kushner, J.P.; Hill, C.P.
Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase
EMBO J.
22
6225-6233
2003
Homo sapiens (P06132)
brenda
Christiansen, L.; Ged, C.; Hombrados, I.; Brons-Poulsen, J.; Fontanellas, A.; de Verneuil, H.; Horder, M.; Petersen, N.E.
Screening for mutations in the uroporphyrinogen decarboxylase gene using denaturing gradient gel electrophoresis. Identification and characterization of six novel mutations associated with familial PCT
Hum. Mutat.
14
222-232
1999
Homo sapiens
brenda
Chaufan, G.; Rios de Molina, M.C.; San Martin de Viale, L.C.
How does hexachlorobenzene treatment affect liver uroporphyrinogen decarboxylase?
Int. J. Biochem. Cell Biol.
33
621-630
2001
Rattus norvegicus
brenda
Martins, B.M.; Grimm, B.; Mock, H.P.; Huber, R.; Messerschmidt, A.
Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism
J. Biol. Chem.
276
44108-44116
2001
Nicotiana tabacum
brenda
Jones, M.A.; Taneja, M.; Xu, Y.; Chung, W.; Stob, C.M.; Lash, T.D.
An effective chromatographic separation of chicken red blood cell coproporphyrinogen oxidase and uroporphyrinogen decarboxylase, two enzymes in heme biosynthesis
Bioorg. Med. Chem. Lett.
14
5559-5564
2004
Gallus gallus
brenda
Nezamzadeh, R.; Seubert, A.; Pohlenz, J.; Brenig, B.
Identification of a mutation in the ovine uroporphyrinogen decarboxylase (UROD) gene associated with a type of porphyria
Anim. Genet.
36
297-302
2005
Ovis aries
brenda
Poblete-Gutierrez, P.; Mendez, M.; Wiederholt, T.; Merk, H.F.; Fontanellas, A.; Wolff, C.; Frank, J.
The molecular basis of porphyria cutanea tarda in Chile: identification and functional characterization of mutations in the uroporphyrinogen decarboxylase gene
Exp. Dermatol.
13
372-379
2004
Homo sapiens
brenda
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
J. Biochem. Mol. Toxicol.
19
19-24
2005
Rattus norvegicus
brenda
Christiansen, L.; Brons-Poulsen, J.; Horder, M.; Brock, A.; Petersen, N.E.
Expression and characterization of six clinically relevant uroporphyrinogen decarboxylase gene mutations
Scand. J. Clin. Lab. Invest.
65
227-235
2005
Homo sapiens
brenda
Juarez, A.B.; Aldonatti, C.; Vigna, M.S.; Rios de Molina, M.d.e.l.C.
Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta)
Can. J. Microbiol.
53
303-312
2007
Parachlorella kessleri
brenda
Fan, J.; Liu, Q.; Hao, Q.; Teng, M.; Niu, L.
Crystal structure of uroporphyrinogen decarboxylase from Bacillus subtilis
J. Bacteriol.
189
3573-3580
2007
Bacillus subtilis
brenda
Phillips, J.D.; Bergonia, H.A.; Reilly, C.A.; Franklin, M.R.; Kushner, J.P.
A porphomethene inhibitor of uroporphyrinogen decarboxylase causes porphyria cutanea tarda
Proc. Natl. Acad. Sci. USA
104
5079-5084
2007
Homo sapiens, Mus musculus
brenda
Cunha, L.; Kuti, M.; Bishop, D.F.; Mezei, M.; Zeng, L.; Zhou, M.M.; Desnick, R.J.
Human uroporphyrinogen III synthase: NMR-based mapping of the active site
Proteins
71
855-873
2007
Homo sapiens
brenda
Wang, Y.; Gatti, P.; Sadilek, M.; Scott, C.R.; Turecek, F.; Gelb, M.H.
Direct assay of enzymes in heme biosynthesis for the detection of porphyrias by tandem mass spectrometry. Uroporphyrinogen decarboxylase and coproporphyrinogen III oxidase
Anal. Chem.
80
2599-2605
2008
Homo sapiens
brenda
Saito, M.; Watanabe, S.; Yoshikawa, H.; Nakamoto, H.
Interaction of the molecular chaperone HtpG with uroporphyrinogen decarboxylase in the cyanobacterium Synechococcus elongatus PCC 7942
Biosci. Biotechnol. Biochem.
72
1394-1397
2008
Synechococcus elongatus
brenda
Remenyik, E.; Lecha, M.; Badenas, C.; Koszo, F.; Vass, V.; Herrero, C.; Varga, V.; Emri, G.; Balogh, A.; Horkay, I.
Childhood-onset mild cutaneous porphyria with compound heterozygotic mutations in the uroporphyrinogen decarboxylase gene
Clin. Exp. Dermatol.
33
602-605
2008
Homo sapiens
brenda
Cribier, B.; Chiaverini, C.; Dali-Youcef, N.; Schmitt, M.; Grima, M.; Hirth, C.; Lacour, J.P.; Chosidow, O.
Porphyria cutanea tarda, hepatitis C, uroporphyrinogen decarboxylase and mutations of HFE gene. A case-control study
Dermatology
218
15-21
2009
Homo sapiens
brenda
Nagaraj, V.A.; Arumugam, R.; Chandra, N.R.; Prasad, D.; Rangarajan, P.N.; Padmanaban, G.
Localisation of Plasmodium falciparum uroporphyrinogen III decarboxylase of the heme-biosynthetic pathway in the apicoplast and characterisation of its catalytic properties
Int. J. Parasitol.
39
559-568
2008
Homo sapiens, Plasmodium falciparum
brenda
Lewis, C.A.; Wolfenden, R.
Uroporphyrinogen decarboxylation as a benchmark for the catalytic proficiency of enzymes
Proc. Natl. Acad. Sci. USA
105
17328-17333
2008
Homo sapiens (P06132), Homo sapiens
brenda
Bergonia, H.A.; Phillips, J.D.; Kushner, J.P.
Reduction of porphyrins to porphyrinogens with palladium on carbon
Anal. Biochem.
384
74-78
2009
Homo sapiens (P06132)
brenda
Warby, C.A.; Phillips, J.D.; Bergonia, H.A.; Whitby, F.G.; Hill, C.P.; Kushner, J.P.
Structural and kinetic characterization of mutant human uroporphyrinogen decarboxylases
Cell. Mol. Biol. (Noisy-le-grand)
55
40-45
2009
Homo sapiens (P06132), Homo sapiens
brenda
Aarsand, A.K.; Boman, H.; Sandberg, S.
Familial and sporadic porphyria cutanea tarda: characterization and diagnostic strategies
Clin. Chem.
55
795-803
2009
Homo sapiens
brenda
Badenas, C.; To-Figueras, J.; Phillips, J.D.; Warby, C.A.; Munoz, C.; Herrero, C.
Identification and characterization of novel uroporphyrinogen decarboxylase gene mutations in a large series of porphyria cutanea tarda patients and relatives
Clin. Genet.
75
346-353
2009
Homo sapiens (P06132), Homo sapiens
brenda
Phillips, J.D.; Warby, C.A.; Whitby, F.G.; Kushner, J.P.; Hill, C.P.
Substrate shuttling between active sites of uroporphyrinogen decarboxylase is not required to generate coproporphyrinogen
J. Mol. Biol.
389
306-314
2009
Homo sapiens (P06132)
brenda
Ryali, M.E.; Whittier, W.L.
Bullous skin lesions in a patient undergoing chronic hemodialysis
Semin. Dial.
23
83-87
2010
Homo sapiens
brenda
To-Figueras, J.; Phillips, J.; Gonzalez-Lopez, J.M.; Badenas, C.; Madrigal, I.; Gonzalez-Romaris, E.M.; Ramos, C.; Aguirre, J.M.; Herrero, C.
Hepatoerythropoietic porphyria due to a novel mutation in the uroporphyrinogen decarboxylase gene
Br. J. Dermatol.
165
499-505
2011
Homo sapiens
brenda
Bushnell, E.A.; Erdtman, E.; Llano, J.; Eriksson, L.A.; Gauld, J.W.
The first branching point in porphyrin biosynthesis: a systematic docking, molecular dynamics and quantum mechanical/molecular mechanical study of substrate binding and mechanism of uroporphyrinogen-III decarboxylase
J. Comput. Chem.
32
822-834
2011
Homo sapiens
brenda
Ito, E.; Yue, S.; Moriyama, E.H.; Hui, A.B.; Kim, I.; Shi, W.; Alajez, N.M.; Bhogal, N.; Li, G.; Datti, A.; Schimmer, A.D.; Wilson, B.C.; Liu, P.P.; Durocher, D.; Neel, B.G.; OSullivan, B.; Cummings, B.; Bristow, R.; Wrana, J.; Liu, F.F.
Uroporphyrinogen decarboxylase is a radiosensitizing target for head and neck cancer
Sci. Transl. Med.
3
67ra7
2011
Homo sapiens
brenda
McDonagh, B.; Pedrajas, J.R.; Padilla, C.A.; Barcena, J.A.
Thiol redox sensitivity of two key enzymes of heme biosynthesis and pentose phosphate pathways: uroporphyrinogen decarboxylase and transketolase
Oxid. Med. Cell. Longev.
2013
932472
2013
Saccharomyces cerevisiae (P32347), Saccharomyces cerevisiae
brenda
Yip, K.W.; Zhang, Z.; Sakemura-Nakatsugawa, N.; Huang, J.W.; Vu, N.M.; Chiang, Y.K.; Lin, C.L.; Kwan, J.Y.; Yue, S.; Jitkova, Y.; To, T.; Zahedi, P.; Pai, E.F.; Schimmer, A.D.; Lovell, J.F.; Sessler, J.L.; Liu, F.F.
A porphodimethene chemical inhibitor of uroporphyrinogen decarboxylase
PLoS ONE
9
e89889
2014
Homo sapiens (P06132)
brenda
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