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Hydroxymethylbilane
Uroporphyrinogen III
hydroxymethylbilane
uroporphyrinogen III + H2O
hydroxymethylbilane
uroporphyrinogen-III + H2O
Preuroporphyrinogen
Uroporphyrinogen III
additional information
?
-
Hydroxymethylbilane
?
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
?
Hydroxymethylbilane
?
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
?
Hydroxymethylbilane
?
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-
-
-
?
Hydroxymethylbilane
?
-
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
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-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
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-
-
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Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
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Hydroxymethylbilane
Uroporphyrinogen III
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-
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?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
enzyme-product structure analysis, overview
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
enzyme-product structure analysis, overview
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
a step in tetrapyrrole biosynthesis, e.g. of chlorophyll, haem, sirohaem and bilins, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
uroporphyrinogen III synthase catalyses the cyclization of HMB with a concomitant inversion of the fourth ring of the porphyrin macrocycle, giving rise to uroporphyrinogen III
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-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
intramolecular rearrangement of the d-pyrrole group and ring closure
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
the D-ring of the hydroxymethylbilane substrate binds to the enzyme in a conformation that shields its terminal portion from reacting with ring A and prevents the formation of the biologically useless uroporphyrinogen I, reaction mechanism, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
the enzyme catalyzes the cyclization and D-ring isomerization of hydroxymethylbilane to uroporphyrinogen III, the cyclic tetrapyrrole and physiologic precursor of heme, chlorophyl, and corrin
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
the enzyme catalyzes the inversion of one of the four heterocyclic rings present in the substrate. Reaction mechanism analysis by high-level quantum mechanical calculations on model systems of the enzyme
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
enzymatic conversion of preuroporphyrinogen. The substrate must bind the enzyme in a conformation that prevents C19 from reacting with C20
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
linear tetrapyrrole
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
linear tetrapyrrole, fourth step in the biosynthesis of porphyrin, essential reaction, decreased enzyme activity leads to the autosomal recessive disorder congenital erythropetic porphyria
macrocyclic uroporphyrinogen III is a precurosr for synthesis of diverse compounds, e.g. heme, siroheme, chlorophyll, F430, and vitamin B12
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
fourth enzyme in heme biosynthesis. Congenital erythropoietic porphyria is a very rare disease that is inherited as an autosomal recessive trait and results from a profound deficiency of uroporphyrinogen III cosynthase, the fourth enzyme in heme biosynthesis. The degree of severity of clinical symptoms mainly depends on the amount of residual uroporphyrinogen III cosynthase activity
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
-
-
?
Preuroporphyrinogen
Uroporphyrinogen III
-
-
-
?
Preuroporphyrinogen
Uroporphyrinogen III
-
-
-
?
Preuroporphyrinogen
Uroporphyrinogen III
-
-
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?
Preuroporphyrinogen
Uroporphyrinogen III
-
-
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?
additional information
?
-
coupled assay method for UROS activity measurement using purified recombinant Pseudomonas aeruginosa porphobilinogen synthase and Bacillus megaterium porphobilinogen deaminase to generate hydroxymethylbilane, the substrate for UROS, enzymatically from 5-aminolaevulinic acid
-
-
?
additional information
?
-
-
coupled assay method for UROS activity measurement using purified recombinant Pseudomonas aeruginosa porphobilinogen synthase and Bacillus megaterium porphobilinogen deaminase to generate hydroxymethylbilane, the substrate for UROS, enzymatically from 5-aminolaevulinic acid
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-
?
additional information
?
-
uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
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-
?
additional information
?
-
-
uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
-
-
?
additional information
?
-
-
hydroxymethylbilane synthase and uroporphyrinogen III synthase catalyze two consecutive reactions, the third and fourth step, in the heme biosynthetic pathway, generating the first linear and the first cyclic tetrapyrroles, respectively. Hydroxymethylbilane synthase, 2.5.1.61, and uroporphyrinogen III synthase may function independently and sequentially with hydroxymethylbilane as a free intermediate, heme biosynthetic pathway, overview. Hypoxia downregulates UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia. Deferoxamine, cobalt chloride, or hypoxia downregulate UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia
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?
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Hydroxymethylbilane
Uroporphyrinogen III
hydroxymethylbilane
uroporphyrinogen III + H2O
hydroxymethylbilane
uroporphyrinogen-III + H2O
additional information
?
-
Hydroxymethylbilane
?
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
?
Hydroxymethylbilane
?
-
synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
-
-
?
Hydroxymethylbilane
?
-
-
-
-
?
Hydroxymethylbilane
?
-
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
Hydroxymethylbilane
Uroporphyrinogen III
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
a step in tetrapyrrole biosynthesis, e.g. of chlorophyll, haem, sirohaem and bilins, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
intramolecular rearrangement of the d-pyrrole group and ring closure
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
the D-ring of the hydroxymethylbilane substrate binds to the enzyme in a conformation that shields its terminal portion from reacting with ring A and prevents the formation of the biologically useless uroporphyrinogen I, reaction mechanism, overview
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
the enzyme catalyzes the cyclization and D-ring isomerization of hydroxymethylbilane to uroporphyrinogen III, the cyclic tetrapyrrole and physiologic precursor of heme, chlorophyl, and corrin
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
?
hydroxymethylbilane
uroporphyrinogen III + H2O
-
-
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
linear tetrapyrrole, fourth step in the biosynthesis of porphyrin, essential reaction, decreased enzyme activity leads to the autosomal recessive disorder congenital erythropetic porphyria
macrocyclic uroporphyrinogen III is a precurosr for synthesis of diverse compounds, e.g. heme, siroheme, chlorophyll, F430, and vitamin B12
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview
-
?
hydroxymethylbilane
uroporphyrinogen-III + H2O
-
fourth enzyme in heme biosynthesis. Congenital erythropoietic porphyria is a very rare disease that is inherited as an autosomal recessive trait and results from a profound deficiency of uroporphyrinogen III cosynthase, the fourth enzyme in heme biosynthesis. The degree of severity of clinical symptoms mainly depends on the amount of residual uroporphyrinogen III cosynthase activity
-
-
?
additional information
?
-
uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
-
-
?
additional information
?
-
-
uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
-
-
?
additional information
?
-
-
hydroxymethylbilane synthase and uroporphyrinogen III synthase catalyze two consecutive reactions, the third and fourth step, in the heme biosynthetic pathway, generating the first linear and the first cyclic tetrapyrroles, respectively. Hydroxymethylbilane synthase, 2.5.1.61, and uroporphyrinogen III synthase may function independently and sequentially with hydroxymethylbilane as a free intermediate, heme biosynthetic pathway, overview. Hypoxia downregulates UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia. Deferoxamine, cobalt chloride, or hypoxia downregulate UROS mRNA expression in hepatic cells, reduction of UROS mRNA is associated with the accumulation of hypoxia-inducible factor 1alpha under normoxia
-
-
?
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C73D
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73L
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73N
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73R/A69E
the mutant shows reduced activity compared to the wild type enzyme
C73R/L43D
the mutant shows slightly increased activity compared to the wild type enzyme
C73Y
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
E127A
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
E249stop
clinical mutation, truncated protein, loss of helix 12
K220A
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
Q249X
-
the mutation is associated with congenital erythropoietic porphyria
R65A
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
S197A
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
S63A
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
T103A
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
T227A
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
T228A
site-directed mutagenesis, conserved residue near to the active site cleft, reduced activity compared to the wild-type enzyme
Y168A
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C73R
0.24% of wild-type activity, homozygous mice are fetal lethals
V99A
5.9% of wild-type activity, homozygous mice are fetal lethals
V99L
14.8% of wild-type activity
E114A
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
E38A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
L116A
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
R164A
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 70% that of the wild-type enzyme
R219A
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 25% that of the wild-type enzyme
E114A
-
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
-
E38A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
-
L116A
-
site-directed mutagenesis, the mutant shows activity slightly reduced compared to the wild-type enzyme
-
R164A
-
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 70% that of the wild-type enzyme
-
R219A
-
site-directed mutagenesis, the mutation causes a decrease in enzymatic activity to about 25% that of the wild-type enzyme
-
D17A
-
60.3% of wild-type activity
E68A
-
82.8% of wild-type activity
H173L
-
106.9% of wild-type activity
K10Q
-
39.7% of wild-type activity
K147Q
-
34.5% of wild-type activity
N121D
-
93.1% of wild-type activity
Y168F
-
1.7% of wild-type activity
Y97F
-
74.1% of wild-type activity
D112G
-
site-directed mutagenesis, 50% reduced activity compared to the wild-type enzyme
R15Q
-
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
S68A
-
site-directed mutagenesis, unaltered activity level compared to the wild-type enzyme
T100A
-
site-directed mutagenesis, 75% reduced activity compared to the wild-type enzyme
Y166F
-
site-directed mutagenesis, more than 99% reduced activity compared to the wild-type enzyme
A104V
a naturally occuring mutation, 60.6% activity compared to the wild-type enzyme
A104V
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
A66V
clinical mutation, altered tertiary structure
A66V
a naturally occuring mutation, 95.6% activity compared to the wild-type enzyme
A66V
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
A69T
a naturally occuring mutation, 24.4% activity compared to the wild-type enzyme
A69T
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
C73A
99% of wild-type activity
C73A
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
C73R
9% of wild-type activity
C73R
a frequent, naturally occuring mutation of a residue of the stabilizing helical region, 14.5% activity compared to the wild-type enzyme
C73R
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria, the mutant protein retains partial catalytic activity but shows reduced the enzyme stability
C73R
-
a naturally occuring mutation in the enzyme responsible for more than one-third of all of the reported cases of the rare autosomal disease congenital erythropoietic porphyria. The mutant protein retains partial catalytic activity but shows reduced the enzyme stability
C73R
the substitution drastically reduces the enzyme activity (1500fold) and stability compared to the wild type enzyme
C73S
78% of wild-type activity
C73S
-
computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants
E81D
a naturally occuring mutation, unaltered activity compared to the wild-type enzyme
E81D
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G188R
a naturally occuring mutation, 41.4% activity compared to the wild-type enzyme
G188R
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G188W
a naturally occuring mutation, 31.6% activity compared to the wild-type enzyme
G188W
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G225S
clinical mutation, altered tertiary structure
G225S
a naturally occuring mutation, 32.4% activity compared to the wild-type enzyme
G225S
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
G236V
a naturally occuring mutation, 34.0% activity compared to the wild-type enzyme
G236V
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
H173Y
a naturally occuring mutation, 72.6% activity compared to the wild-type enzyme
H173Y
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
I129T
clinical mutation, altered tertiary structure
I129T
a naturally occuring mutation, 20.0% activity compared to the wild-type enzyme
I129T
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
I219S
a naturally occuring mutation, 85.0% activity compared to the wild-type enzyme
I219S
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
L237P
a naturally occuring mutation, 57.9% activity compared to the wild-type enzyme
L237P
-
the mutation is associated with congenital erythropoietic porphyria
L237P
the mutation is associated with congenital erythropoietic porphyria
L237P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
L4F
clinical mutation, altered tertiary structure
L4F
a naturally occuring mutation, 20.2% activity compared to the wild-type enzyme
L4F
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
P248Q
clinical mutation, altered tertiary structure
P248Q
a naturally occuring mutation, 29.2% activity compared to the wild-type enzyme
P248Q
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
P53L
clinical mutation, altered tertiary structure
P53L
a naturally occuring mutation, inactive mutant, no purification of the recombinant mutant
P53L
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
Q187P
a naturally occuring mutation, 15.0% activity compared to the wild-type enzyme
Q187P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
S212P
clinical mutation, altered tertiary structure
S212P
a naturally occuring mutation, 20.0% activity compared to the wild-type enzyme
S212P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
S47P
a naturally occuring mutation, unaltered activity compared to the wild-type enzyme
S47P
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
T228M
clinical mutation, altered tertiary structure
T228M
a naturally occuring mutation, 97.5% activity compared to the wild-type enzyme
T228M
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
T62A
site-directed mutagenesis, conserved residue near to the active site cleft, unaltered activity level compared to the wild-type enzyme
T62A
a naturally occuring mutation, 1.2% activity compared to the wild-type enzyme
T62A
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
V3F
clinical mutation, altered tertiary structure
V3F
a naturally occuring mutation, 19.3% activity compared to the wild-type enzyme
V3F
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
V82F
a naturally occuring mutation, 93.8% activity compared to the wild-type enzyme
V82F
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
V99A
a naturally occuring mutation, 88.2% activity compared to the wild-type enzyme
V99A
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
Y19C
clinical mutation, altered tertiary structure
Y19C
a naturally occuring mutation, 13.1% activity compared to the wild-type enzyme
Y19C
-
a naturally occuring mutation in the enzyme involved in congenital erythropoietic porphyria
additional information
-
16 known mutations causing congenital erythropoietic porphyria in humans via alterations of the tertiary enzyme structure
additional information
the naturally occuring clinical mutations lead to loss in activity due to structural alterations in the enzymes, overview
additional information
-
the naturally occuring clinical mutations lead to loss in activity due to structural alterations in the enzymes, overview
additional information
-
identification of mutations in the uroporphyrinogen III cosynthase gene in German patients with congenital erythropoietic porphyria. Identification of four different mutations: C73R, a hotspot mutation, the promoter mutation 86A, and two missense mutations, designated G236V and L237P, the latter one encounters in the homozygous state in one of the patients
additional information
changes in the unfolding rate, relative to wild type, overview. Cloning, expression, and analysis of 25 missense mutants from congenital erythropoietic porphyria, CEP, patients, genotyping, overview
additional information
-
changes in the unfolding rate, relative to wild type, overview. Cloning, expression, and analysis of 25 missense mutants from congenital erythropoietic porphyria, CEP, patients, genotyping, overview
additional information
-
genotype/phenotype analysis of the studied cases of congenital erythropoietic porphyria, overview
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Hart, G.J.; Battersby, A.R.
Purification and properties of uroporphyrinogen III synthase (co-synthase) from Euglena gracilis
Biochem. J.
232
151-160
1985
Euglena gracilis
brenda
Tsai, S.F.; Bishop, D.F.; Desnick, R.J.
Purification and properties of uroporphyrinogen III synthase from human erythrocytes
J. Biol. Chem.
262
1268-1273
1987
Homo sapiens
brenda
Clement, R.P.; Kohashi, M.; Piper, W.N.
Rat hepatic uroporphyrinogen III cosynthase: Purification, properties and inhibition by metal ions
Arch. Biochem. Biophys.
214
657-667
1982
Rattus norvegicus
brenda
Kohashi, M.; Clement, R.P.; Tse, J.; Piper, W.N.
Rat hepatic uroporphyrinogen III co-synthase. Purification and evidence for a bound folate coenzyme participating in the biosynthesis of uroprphyrinogen III
Biochem. J.
220
755-765
1984
Rattus norvegicus
brenda
Alwan, A.F.; Jordan, P.M.
Isolation of uroporphyrinogen III synthase from Escherichia coli
Biochem. Soc. Trans.
16
965-966
1988
Escherichia coli
-
brenda
Smythe, E.; Williams, D.C.
Rat liver uroporphyrinogen III synthase has similar properties to the enzyme from Euglena gracilis, including absence of a requirement for a reversibly bound cofactor for activity
Biochem. J.
253
275-279
1988
Rattus norvegicus
brenda
Levin, E.Y.
Enzymatic properties of uroporphyrinogen III cosynthetase
Biochemistry
10
4669-4675
1971
Mus musculus
brenda
Wright, D.J.; Lim, C.K.
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Homo sapiens (P10746), Homo sapiens
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Homo sapiens (P10746), Homo sapiens
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