EC Number   |
General Information |
Reference |
|---|
    4.2.1.75 | evolution |
evolution of the segment swapped topology facilitates the evolution of enzyme function for this protein by influencing its dynamic properties |
749259 |
| 4.2.1.75 | malfunction |
congenital erythropoietic porphyria is a rare autosomal disease ultimately related to deleterious mutations in uroporphyrinogen III synthase. In absence or dysfunction of the enzyme, hydroxymethylbilane spontaneously degrades to the by-product uroporphyrinogen I, which cannot lead to the heme group and accumulates in the body, producing some of the symptoms observed in congenital erythropoietic porphyria patients, phenotype, structural and molecular basis, overview |
713692 |
| 4.2.1.75 | malfunction |
congenital erythropoietic porphyria is the rarest autosomal recessive porphyria resulting from a deficiency of uroporphyrinogen III cosynthase |
730358 |
| 4.2.1.75 | malfunction |
congenital erythropoietic porphyria results from a deficiency in uroporphyrinogen III synthase enzyme activity |
729813 |
| 4.2.1.75 | malfunction |
deficiency of uroporphyrinogen III synthase (UROS) causes congenital erythropoietic porphyria. The disease, originating from the inheritance of mutations within the UROS gene, presents a recessive form of transmission |
747439 |
| 4.2.1.75 | metabolism |
S-adenosyl-L-methionine uroprophyrinogen III methyltransferase/synthase is a key bifunctional enzyme in the biosynthesis of cobalamin and other tetrapyrrols |
-, 714579 |
| 4.2.1.75 | metabolism |
U3S is one of the key enzymes in the biosynthesis of tetrapyrrole compounds |
-, 714059 |
| 4.2.1.75 | physiological function |
U3S catalyzes the cyclization of the linear hydroxymethylbilane to uroporphyrinogen III. Arg219 is the key residue important for the catalytic activity of psU3S, Tyr162 is important for activity |
-, 714059 |
| 4.2.1.75 | physiological function |
UROIIIS catalyzes the cyclization of the linear tetrapyrrole hydroxymethylbilane to produce uroporphyrin III. A Cys in position 73 is not essential for the catalytic activity of the enzyme but its mutation to Arg speeds up the process of irreversible unfolding and aggregation |
715590 |
| 4.2.1.75 | physiological function |
UROIIIS is the fourth enzyme of the biosynthetic route of the heme group and catalyzes the cyclization of the linear tetrapyrrol hydroxymethylbilane, inverting the configuration in one of the aromatic rings. It accelerates the production of uroporphyrinogen III (an energetically unfavorable chemical reaction) at the same time as it suppresses the spontaneous reaction pathway to yield uroporphyrinogen I |
713692 |
