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Information on EC 4.1.1.37 - uroporphyrinogen decarboxylase and Organism(s) Homo sapiens and UniProt Accession P06132

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     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.37 uroporphyrinogen decarboxylase
IUBMB Comments
Acts on a number of porphyrinogens.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P06132
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected 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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
uroporphyrinogen decarboxylase
-
Decarboxylase, uroporphyrinogen
-
-
-
-
Porphyrinogen carboxy-lyase
-
-
-
-
UPD
-
-
-
-
URO-D
Uro-decarboxylase
-
-
UROD1
-
-
uroporphyrinogen decarboxylase
-
-
uroporphyrinogen decarboxylase 1
-
-
Uroporphyrinogen III decarboxylase
-
-
-
-
uroporphyrinogen-decarboxylase
-
-
uroporphyrinogen-III decarboxylase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
uroporphyrinogen-III carboxy-lyase (coproporphyrinogen-III-forming)
Acts on a number of porphyrinogens.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-70-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pentacarboxylic porphyrinogen I
coproporphyrinogen-I + 4 CO2
show the reaction diagram
-
-
-
?
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
show the reaction diagram
uroporphyrinogen-I
coproporphyrinogen-I + 4 CO2
show the reaction diagram
uroporphyrinogen-III
coproporphyrinogen-III + 4 CO2
show the reaction diagram
5-COOH-porphyrinogen I
?
show the reaction diagram
-
-
-
-
?
5-COOH-porphyrinogen I
Coproporphyrinogen I + CO2
show the reaction diagram
-
-
-
-
?
5-COOH-porphyrinogen III
Coproporphyrinogen III + CO2
show the reaction diagram
-
-
-
-
?
7-COOH-porphyrinogen I
Coproporphyrinogen I + CO2
show the reaction diagram
-
-
-
-
?
7-COOH-porphyrinogen III
Coproporphyrinogen III + CO2
show the reaction diagram
-
-
-
-
?
8-COOH-porphyrinogen III
Coproporphyrinogen III + CO2
show the reaction diagram
-
-
-
-
?
heptaporphyrinogen III
hexaporphyrinogen III + CO2
show the reaction diagram
-
formation of the stepwise decarboxylation products, hepta-, hexa-, penta-, and coproporphyrinogen III
-
-
?
hexaporphyrinogen III
pentaporphyrinogen III + CO2
show the reaction diagram
-
formation of the stepwise decarboxylation products, hepta-, hexa-, penta-, and coproporphyrinogen III
-
-
?
uroporphyrinogen I
coproporphyrinogen I + 4 CO2
show the reaction diagram
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
show the reaction diagram
uroporphyrinogen III
heptaporphyrinogen III + CO2
show the reaction diagram
-
formation of the stepwise decarboxylation products, hepta-, hexa-, penta-, and coproporphyrinogen III
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
show the reaction diagram
uroporphyrinogen-III
coproporphyrinogen-III + 4 CO2
show the reaction diagram
Uroporphyrinogen III
Coproporphyrinogen III + 4 CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
-
7-COOH-porphyrinogen I
-
inhibits decarboxylation of 7-COOH-porphyrinogen III
7-COOH-porphyrinogen III
-
inhibits decarboxylation of 7-COOH-porphyrinogen I
Butanedione
-
-
diethyldicarbonate
-
reversed by hydroxylamine
Fe2+
-
weak
iodoacetamide
-
-
p-hydroxymercuribenzoate
-
-
PCMB
-
-
Phenylglyoxal
-
-
porphomethene
-
competitive inhibitor
Sn2+
-
weak
Uroporphyrinogen I
uroporphyrinogen III
-
inhibits decarboxylation of uroporphyrinogen I, no inhibition of 7-COOH-series II porphyrinogens and 5-COOH-series II porphyrinogens decarboxylation
Zn2+
-
weak
additional information
not inhibited by acebutulol, naproxen, verapramil, and furosemide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Reducing agents
-
required
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0277 - 0.0381
uroporphyrinogen-I
0.0108 - 0.0148
uroporphyrinogen-III
0.00007 - 0.00215
5-COOH-porphyrinogen I
0.00005 - 0.0004
5-COOH-porphyrinogen III
0.00231
7-COOH, porphyrinogen
-
isoenzyme UROD54000
0.000231 - 0.00071
7-COOH-porphyrinogen
0.00085
7-COOH-porphyrinogen I
-
-
0.00035
7-COOH-porphyrinogen III
-
-
0.00025 - 0.00053
8-COOH-porphyrinogen III
0.0008 - 0.00533
Uroporphyrinogen I
0.00035 - 0.00072
uroporphyrinogen III
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.102 - 0.124
uroporphyrinogen-I
0.317 - 0.425
uroporphyrinogen-III
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0099
PI-16
Homo sapiens
in 0.1 M Tris, pH 7.7, 7.5 mM dithiothreitol, at 37°C`
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0018
-
-
0.0583
-
-
0.17
-
-
0.75
-
crude enzyme, at 37°C
7.6
-
purified enzyme, at 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
with uroporphyrinogen III or 5-COOH-porphyrinogen III as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 8
-
in 0.2 M KH2PO4, 0.1 mM dithiothreitol
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
malfunction
metabolism
-
UROD is a key regulator of heme biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCUP_HUMAN
367
0
40787
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
84000
SDS-PAGE scURO-D-protein
86000
analytical ultracentrifugation scURO-D
34000
-
isoenzyme II, gel filtration
35000
39500
-
x * 39500, SDS-PAGE
40831
-
x * 40831, calculation from nucleotide sequence
41000
-
SDS-PAGE
41070
44000
-
x * 44000, uroporphyrinogen decarboxylase containing a histidine tag on the amino terminal end, SDS-PAGE
46000
-
1 * 46000, SDS-PAGE
52000
-
1 * 52000, isoenzyme I, SDS-PAGE
52000 - 54000
-
isoenzyme I, gel filtration
54000
-
x * 54000, isoenzyme UROD54000, SDS-PAGE
58000
-
gel filtration
66000
-
uroporphyrinogen decarboxylase containing a histidine tag on the amino terminal end, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
SDS-PAGE, the dimeric structure of uroporphyrinogen decarboxylase is required to achieve conformational stability and to create a large active-site cleft
dimer
-
Superdex-G200 gel filtration
homodimer
-
-
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
mutant URO-D proteins G156D, F232L, and I260T
recombinant mutant proteins K297N and G318R
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A22V
soluble but reduced catalytic activity
D306Y
mutation results in an insoluble recombinant protein
D79N
misfolded protein that is trafficked to inclusion bodies
D86
site-directed mutagenesis
D86E
site-directed mutagenesis
D86G
site-directed mutagenesis
F217Y
F84I
soluble but reduced catalytic activity
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
P150L
misfolded protein that is trafficked to inclusion bodies
Q116X
this may yield a truncated protein of 115 amino acids or nonsense-mediated mRNA decay
T141I
soluble but reduced catalytic activity
Y164F
site-directed mutagenesis
Y164G
Y182C
soluble but reduced catalytic activity
A80S
-
less than 12% of the specific activity of wild-type enzyme, Q38R-glutathione S-transferase fusion protein
C705A
-
site-directed mutagenesis
F229L
-
site-directed mutagenesis
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
G281E
-
the mutation is associated with hepatoerythropoietic porphyria
M01T
-
site-directed mutagenesis
M1V/P235S
-
the mutation is associated with UROD deficiency
M324T
-
site-directed mutagenesis
Q206X
-
inactive mutant, Q38R-glutathione S-transferase fusion protein
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
T20C
-
site-directed mutagenesis
T989C
-
site-directed mutagenesis
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 60
-
-
60
-
20 min, 52% loss of activity of the liver enzyme, 55% loss of activity of the erythrocyte enzyme
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid inactivation by uroporphyrin-catalyzed photooxidation
-
4440
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant URO-D proteins G156D, F232L, and I260T
Ni-NTA column
Ni-NTA column chromatography and gel filtration
IMAC column chromatography, Mono Q column chromatography, and Superdex 70 gel filtration
-
isoenzymes I and II
-
Ni-NTA column chromatography
-
wild-type and mutant enzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned, sequenced and expressed in Escherichia coli
expressed in Escherichia coli BL21-pLysS
expressed in Escherichia coli BL21-RIL(DE3) cells
expression in Escherichia coli
expression in Escherichia coli as His-tagged enzyme
uroporphyrinogen decarboxylase mutations G318R, D306Y and K297N
expressed in Escherichia coli Rosetta2 cells
-
expressed in Escherichia coli strain Top10
-
expression in Escherichia coli
-
wild-type enzyme and mutants causing porphyria cutanea tarda, expression in Escherichia coli BL-21
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
UROD is significantly overexpressed in head and neck cancer patient biopsies
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
subnormal activity of uroporphyrinogen decarboxylase in hepatocytes is responsible for the most common form of porphyria in humans, porphyria cutanea tarda
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Elder, G.H.; Tovey, J.A.; Sheppard, D.M.
Purification of uroporphyrinogen decarboxylase from human erythrocytes
Biochem. J.
215
45-55
1983
Homo sapiens
Manually annotated by BRENDA team
Elder, G.H.; Urquhart, A.J.
Human uroporphyrinogen decarboxylase. Do tissue-specific isoenzymes exist?
Biochem. Soc. Trans.
12
663-664
1984
Homo sapiens
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Roberts, A.G.; Elder, G.H.
Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes
Methods Enzymol.
281
349-355
1997
Homo sapiens
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Elder, G.H.; Roberts, A.G.
Uroporphyrinogen decarboxylase
J. Bioenerg. Biomembr.
27
207-214
1995
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Ryali, M.E.; Whittier, W.L.
Bullous skin lesions in a patient undergoing chronic hemodialysis
Semin. Dial.
23
83-87
2010
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team