UROS Human
Uroporphyrinogen-III synthase, UROIIIS, UROS, Hydroxymethylbilane hydrolyase [cyclizing], Uroporphyrinogen-III cosynthase.
Description
UROS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-265 a.a.) and having a molecular mass of 30.7kDa.
UROS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
The enzyme Uroporphyrinogen III synthase (UROS) plays a crucial role in the fourth step of porphyrin metabolism, specifically in converting hydroxymethyl bilane to uroporphyrinogen III. Deficiencies in the UROS protein can result in molecular abnormalities, leading to the autosomal recessive Gunther disease, also known as congenital erythropoietic porphyria (CEP).
Uroporphyrinogen III synthase (UROS) derived from E. coli is a single, non-glycosylated polypeptide chain comprising 285 amino acids (specifically, amino acids 1 to 265). This protein has a molecular weight of 30.7 kDa. Notably, a 20 amino acid His-tag is fused to the N-terminus of the UROS protein, and its purification is achieved through proprietary chromatographic techniques.
The provided UROS protein solution has a concentration of 1 mg/ml. It is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 10% glycerol, and 0.1M NaCl.
While the UROS Human Recombinant protein remains stable at 4°C for a duration of 1 week, it is recommended to store it at temperatures below -18°C for optimal long-term preservation. It's essential to avoid repeated freeze-thaw cycles to maintain the protein's integrity and activity.
Uroporphyrinogen-III synthase, UROIIIS, UROS, Hydroxymethylbilane hydrolyase [cyclizing], Uroporphyrinogen-III cosynthase.
MGSSHHHHHH SSGLVPRGSH MKVLLLKDAK EDDCGQDPYI RELGLYGLEA TLIPVLSFEF LSLPSFSEKL SHPEDYGGLI FTSPRAVEAA ELCLEQNNKT EVWERSLKEK WNAKSVYVVG NATASLVSKI GLDTEGETCG NAEKLAEYIC SRESSALPLL FPCGNLKREI LPKALKDKGI AMESITVYQT VAHPGIQGNL NSYYSQQGVP ASITFFSPSG LTYSLKHIQE LSGDNIDQIK FAAIGPTTAR ALAAQGLPVS CTAESPTPQA LATGIRKALQ PHGCC.
Product Science Overview
Uroporphyrinogen III Synthase (UROS) is a crucial enzyme in the heme biosynthetic pathway. It catalyzes the conversion of hydroxymethyl bilane into uroporphyrinogen III, a key precursor in the synthesis of heme, chlorophyll, and other tetrapyrroles . The recombinant form of this enzyme, produced through genetic engineering, is used extensively in research and therapeutic applications.
Uroporphyrinogen III Synthase is a monomeric protein with an approximate molecular mass of 29.5 kDa . The enzyme folds into two alpha/beta domains connected by a beta-ladder, with the active site located between these domains . This structural arrangement is essential for its catalytic activity, which involves the inversion of the final pyrrole unit (ring D) of the linear tetrapyrrole molecule, linking it to the first pyrrole unit (ring A) to form the macrocyclic structure, uroporphyrinogen III .
The enzyme plays a pivotal role in the heme biosynthesis pathway. The pathway begins with the synthesis of 5-aminolevulinic acid (ALA), which is then converted into porphobilinogen (PBG). Four molecules of PBG are condensed to form hydroxymethyl bilane, which is subsequently cyclized by UROS to produce uroporphyrinogen III . This compound is then further modified to produce heme and other tetrapyrroles.
Deficiency in Uroporphyrinogen III Synthase activity is associated with a rare genetic disorder known as congenital erythropoietic porphyria (CEP), also known as Gunther’s disease . This autosomal recessive disorder results in the accumulation of uroporphyrin I and coproporphyrin I, leading to severe photosensitivity, hemolytic anemia, and other systemic complications .
The recombinant form of Uroporphyrinogen III Synthase is produced using various expression systems, including bacterial, yeast, and mammalian cells. This recombinant enzyme is used in research to study the heme biosynthesis pathway and to develop therapeutic strategies for disorders like CEP . The purification process involves multiple chromatographic steps to achieve high purity and activity .
