Cloned (Comment) | Organism |
---|---|
stably expression of GFP-tagged UROIIIS-WT or UROIIIS-C73R proteins in MLP29cell lines, reduced expression levels of C73R-UROIIIS in the mammalian cells | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C73A | computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants | Homo sapiens |
C73D | computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants | Homo sapiens |
C73L | computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants | Homo sapiens |
C73N | computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants | Homo sapiens |
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 | Homo sapiens |
C73S | computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants | Homo sapiens |
C73Y | computational modeling, structure comparison with the wild-type enzyme and the other C73 mutants | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
hydroxymethylbilane | Homo sapiens | - |
uroporphyrinogen III + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hydroxymethylbilane | - |
Homo sapiens | uroporphyrinogen III + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
UROIIIS | - |
Homo sapiens |
Uroporphyrinogen III synthase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
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 | Homo sapiens |