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Uroporphyrinogen III synthase

uroporphyrinogen III synthase, UROS, UROIIIS, uroporphyrinogen III cosynthetase
The protein encoded by this gene catalyzes the fourth step of porphyrin biosynthesis in the heme biosynthetic pathway. Defects in this gene cause congenital erythropoietic porphyria (Gunther's disease). [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, STEP, ferrochelatase
Papers on uroporphyrinogen III synthase
Comprehensive characterization of the effects of ellagic acid and urolithins on colorectal cancer and key associated molecular hallmarks: microRNA-cell specific induction of CDKN1A (p21) as a common mechanism involved.
Espín et al., Murcia, Spain. In Mol Nutr Food Res, Jan 2016
SCOPE: Ellagitannins (ETs), ellagic acid (EA), and the colonic metabolites urolithins (Uros) exhibit anticancer effects against colon cells but a comprehensive molecular analysis has not been done.
Inducing iron deficiency improves erythropoiesis and photosensitivity in congenital erythropoietic porphyria.
Abkowitz et al., Seattle, United States. In Blood, Aug 2015
Congenital erythropoietic porphyria (CEP) is an autosomal recessive disorder of heme synthesis characterized by reduced activity of uroporphyrinogen III synthase and the accumulation of nonphysiologic isomer I porphyrin metabolites, resulting in ineffective erythropoiesis and devastating skin photosensitivity.
Effects of bisphenol A on chlorophyll synthesis in soybean seedlings.
Huang et al., Wuxi, China. In Environ Sci Pollut Res Int, Apr 2015
Exposure to 1.5 mg/L BPA decreased the 5-aminolevulinic acid (ALA) content and increased protoporphyrin IX (Proto IX), magnesium protoporphyrin, and protochlorophyll contents and 5-aminolaevulinic acid dehydratase, porphobilinogen deaminase, uroporphyrinogen III synthase, uroporphyrinogen III decarboxylase, and protoporphyrinogen oxidase activities.
Tuning intracellular homeostasis of human uroporphyrinogen III synthase by enzyme engineering at a single hotspot of congenital erythropoietic porphyria.
Millet et al., Bilbao, Spain. In Hum Mol Genet, 2014
Congenital erythropoietic porphyria (CEP) results from a deficiency in uroporphyrinogen III synthase enzyme (UROIIIS) activity that ultimately stems from deleterious mutations in the uroS gene.
Therapeutic potential of proteasome inhibitors in congenital erythropoietic porphyria.
Richard et al., Bordeaux, France. In Proc Natl Acad Sci U S A, 2013
Congenital erythropoietic porphyria (CEP) is a rare autosomal recessive disorder characterized by uroporphyrinogen III synthase (UROS) deficiency resulting in massive porphyrin accumulation in blood cells, which is responsible for hemolytic anemia and skin photosensitivity.
Congenital Erythropoietic Porphyria
Desnick et al., Seattle, United States. In Unknown Journal, 2013
The diagnosis is confirmed most commonly by the presence of biallelic UROS mutations or on rare occasion by the identification of a hemizygous mutation in the X-linked gene GATA1.
Comparative analysis of genome sequences from four strains of the Buchnera aphidicola Mp endosymbion of the green peach aphid, Myzus persicae.
Wilson et al., Coral Gables, United States. In Bmc Genomics, 2012
These include genes encoding five enzymes required for biosynthesis of the modified nucleoside queosine, the heme pathway enzyme uroporphyrinogen III synthase, and asparaginase.
Mutational analysis of uroporphyrinogen III cosynthase gene in Iranian families with congenital erythropoietic porphyria.
Abbaszadegan et al., Mashhad, Iran. In Mol Biol Rep, 2012
A, T to C change at nucleotide 34313, leading to a substitution of Leucine by Proline at codon 237, was observed in the homozygous state in a family with congenital erythropoietic porphyria.
Intracellular rescue of the uroporphyrinogen III synthase activity in enzymes carrying the hotspot mutation C73R.
Millet et al., Spain. In J Biol Chem, 2011
Intracellular rescue of the uroporphyrinogen III synthase activity in enzymes carrying the hotspot mutation C73R.
Structural, thermodynamic, and mechanistical studies in uroporphyrinogen III synthase: molecular basis of congenital erythropoietic porphyria.
Millet et al., Spain. In Adv Protein Chem Struct Biol, 2010
REVIEW: Structural, thermodynamic, and mechanistical studies in uroporphyrinogen III synthase and molecular basis of congenital erythropoietic porphyria
Congenital erythropoietic porphyria: a novel uroporphyrinogen III synthase branchpoint mutation reveals underlying wild-type alternatively spliced transcripts.
Desnick et al., New York City, United States. In Blood, 2010
Data show that branchpoint sequence (BPS)mutation reduced the wild-type transcript and UROS enzyme activity in CEP lymphoblasts to approximately 10% and 15% of normal, respectively.
Characterization of DUF724 gene family in Arabidopsis thaliana.
Ye et al., Beijing, China. In Plant Mol Biol, 2010
Data show that AtDuf3 genes were expressed in roots, leaves, shoot apical meristems, anthers and pollen grains. They may form homodimers or homopolymers, but did not interact with other members of the same family.
Congenital erythropoietic porphyria: mutation update and correlations between genotype and phenotype.
de Verneuil et al., Bordeaux, France. In Cell Mol Biol (noisy-le-grand), 2008
High quality genotype/phenotype analysis is a difficult issue in rare genetic diseases such as congenital erythropoietic porphyria (CEP) or Günther's disease, a heme biosynthesis defect due to uroporphyrinogen III synthase deficiency.
Congenital erythropoietic porphyria associated with myelodysplasia presenting in a 72-year-old man: report of a case and review of the literature.
Lim et al., Detroit, United States. In Br J Dermatol, 2003
Congenital erythropoietic porphyria (CEP) is a rare autosomal recessive disease owing to the deficient activity of uroporphyrinogen III synthase, the fourth enzyme in the porphyrin-haem synthetic pathway.
Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase.
Warren et al., Salt Lake City, United States. In Biochem Soc Trans, 2002
The final common biosynthetic step in tetrapyrrole biosynthesis is the generation of uroporphyrinogen by uroporphyrinogen III synthase, whereby the D ring of hydroxymethylbilane is flipped during ring closure to generate the asymmetrical structure of uroporphyrinogen III.
A gene cluster inChlorobium vibrioforme encoding the first enzymes of chlorophyll biosynthesis.
Avissar et al., Providence, United States. In Photosynth Res, 1994
ThehemA, hemC andhemD genes encode the enzymes glutamyl tRNA dehydrogenase, porphobilinogen deaminase and uroporphyrinogen III synthase, respectively.
Bone-marrow transplantation for congenital erythropoietic porphyria.
Weinkove et al., Manchester, United Kingdom. In Lancet, 1991
Congenital erythropoietic porphyria, a disorder of haem synthesis, is caused by uroporphyrinogen III synthase deficiency in bone-marrow normoblasts.
Uroporphyrinogen 3 cosynthetase activity in the fox squirrel (Sciurus niger).
Flyger et al., In Science, 1971
The activity of uroporphyrinogen III cosynthetase in hemolyzates and tissue extracts from fox squirrels is much less than in similar preparations from gray squirrels.
Uroporphyrinogen 3 cosynthetase in bovine erythropoietic porphyria.
Levin, In Science, 1968
The activity of uroporphyrinogen III cosynthetase is much lower in hemolyzates from mature cattle with congenital erythropoietic porphyria than in hemolyzates from mature normal cattle.
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