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Synonyms
uros, uroporphyrinogen iii synthase, porphobilinogenase, uro-synthase, uroiiis, uroporphyrinogen iii cosynthase, u3s, uro synthase, uroporphyrinogen-iii synthase, uro'gen iii synthase,
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Hydroxymethylbilane hydrolyase [cyclizing]
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hydroxymethylbilane hydrolyase, cyclizing
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Isomerase, uroporphyrinogen
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Porphobilinogenase
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Synthase, uroporphyrinogen III co-
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Uroporphyrinogen III co-synthase
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Uroporphyrinogen III cosynthase
Uroporphyrinogen III synthase
Uroporphyrinogen isomerase
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Uroporphyrinogen-III cosynthase
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Uroporphyrinogen-III cosynthetase
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uroporphyrinogen-III-synthase
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CobA/HemD
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U3S
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URO-synthase
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UROIIIS
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Uroporphyrinogen III cosynthase
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Uroporphyrinogen III cosynthase
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Uroporphyrinogen III cosynthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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Uroporphyrinogen III synthase
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UROS
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hydroxymethylbilane = uroporphyrinogen III + H2O
hydroxymethylbilane = uroporphyrinogen III + H2O
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hydroxymethylbilane = uroporphyrinogen III + H2O
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure
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hydroxymethylbilane = uroporphyrinogen III + H2O
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure
hydroxymethylbilane = uroporphyrinogen III + H2O
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, Tyr166 is essential for catalysis and/or substrate binding
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hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism via azafulvene and azofulvene intermediates, the product binds between the two domains and is held in place by a network of hydrogen bonds between the products side chain carboxylates and the proteins main chain amides. Interactions of the product A and B ring carboxylate side chains with both structural domains of U3S appear to dictate the relative orientation of the domains in the closed enzyme conformation and likely remain intact during catalysis. The product C and D rings are less constrained in the structure, consistent with the conformational changes required for the catalytic cyclization with inversion of D ring orientation. A conserved tyrosine residue is potentially positioned to facilitate loss of a hydroxyl from the substrate to initiate the catalytic reaction, overview
hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism, modelling, overview
hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism, modeling involving Tyr168, overview
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hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism via azafulvene and azofulvene intermediates, the product binds between the two domains and is held in place by a network of hydrogen bonds between the products side chain carboxylates and the proteins main chain amides. Interactions of the product A and B ring carboxylate side chains with both structural domains of U3S appear to dictate the relative orientation of the domains in the closed enzyme conformation and likely remain intact during catalysis. The product C and D rings are less constrained in the structure, consistent with the conformational changes required for the catalytic cyclization with inversion of D ring orientation. A conserved tyrosine residue is potentially positioned to facilitate loss of a hydroxyl from the substrate to initiate the catalytic reaction, overview
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Hydroxymethylbilane
Uroporphyrinogen III
hydroxymethylbilane
uroporphyrinogen III + H2O
hydroxymethylbilane
uroporphyrinogen-III + H2O
Preuroporphyrinogen
Uroporphyrinogen III
additional information
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Hydroxymethylbilane
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synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
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Hydroxymethylbilane
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synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
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Hydroxymethylbilane
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Hydroxymethylbilane
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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enzyme-product structure analysis, overview
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Hydroxymethylbilane
Uroporphyrinogen III
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enzyme-product structure analysis, overview
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Hydroxymethylbilane
Uroporphyrinogen III
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hydroxymethylbilane
uroporphyrinogen III + H2O
a step in tetrapyrrole biosynthesis, e.g. of chlorophyll, haem, sirohaem and bilins, overview
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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
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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intramolecular rearrangement of the d-pyrrole group and ring closure
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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
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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
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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
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hydroxymethylbilane
uroporphyrinogen III + H2O
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enzymatic conversion of preuroporphyrinogen. The substrate must bind the enzyme in a conformation that prevents C19 from reacting with C20
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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linear tetrapyrrole
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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
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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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
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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Preuroporphyrinogen
Uroporphyrinogen III
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Preuroporphyrinogen
Uroporphyrinogen III
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Preuroporphyrinogen
Uroporphyrinogen III
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Preuroporphyrinogen
Uroporphyrinogen III
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additional information
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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
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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
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uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
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additional information
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uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
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additional information
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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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Hydroxymethylbilane
Uroporphyrinogen III
hydroxymethylbilane
uroporphyrinogen III + H2O
hydroxymethylbilane
uroporphyrinogen-III + H2O
additional information
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Hydroxymethylbilane
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synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
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Hydroxymethylbilane
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synthesis of uroporphyrinogen III, key intermediate for biosynthesis of tetrapyrrolic compounds like chlorophylls, hemes, cytochromes and vitamin B12
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Hydroxymethylbilane
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Hydroxymethylbilane
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Hydroxymethylbilane
Uroporphyrinogen III
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Hydroxymethylbilane
Uroporphyrinogen III
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hydroxymethylbilane
uroporphyrinogen III + H2O
a step in tetrapyrrole biosynthesis, e.g. of chlorophyll, haem, sirohaem and bilins, overview
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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intramolecular rearrangement of the d-pyrrole group and ring closure
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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
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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
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hydroxymethylbilane
uroporphyrinogen III + H2O
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hydroxymethylbilane
uroporphyrinogen III + H2O
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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
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview
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hydroxymethylbilane
uroporphyrinogen-III + H2O
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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
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additional information
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uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
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additional information
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uroporphyrinogen III synthase functions as heme synthesis enzyme during hematopoietic development of Danio rerio
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additional information
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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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0.00015 - 10
Hydroxymethylbilane
additional information
additional information
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0.00015
Hydroxymethylbilane
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pH not specified in the publication, temperature not specified in the publication
0.00033
Hydroxymethylbilane
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0.005
Hydroxymethylbilane
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0.005 - 0.02
Hydroxymethylbilane
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0.01 - 0.02
Hydroxymethylbilane
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0.012 - 0.04
Hydroxymethylbilane
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0.05
Hydroxymethylbilane
mutant enzyme C73R/A69E, pH and temperature not specified in the publication
0.06
Hydroxymethylbilane
wild type enzyme, pH and temperature not specified in the publication
0.07
Hydroxymethylbilane
mutant enzyme C73R/L43D, pH and temperature not specified in the publication
1.01
Hydroxymethylbilane
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10
Hydroxymethylbilane
Km above 10 mM, mutant enzyme C73R, pH and temperature not specified in the publication
additional information
additional information
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additional information
additional information
enzyme kinetics in relation to enzyme stability of wild-type and mutant enzymes, wild-type UROIIIS Is a kinetically stable protein, overview
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additional information
additional information
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enzyme kinetics in relation to enzyme stability of wild-type and mutant enzymes, wild-type UROIIIS Is a kinetically stable protein, overview
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additional information
additional information
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kinetic and thermodynamic analysis, thermodynamic versus kinetic stability, overview
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4.2.1.75 uroporphyrinogen-III synthase
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