Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli as His-tagged enzyme | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
modified enzyme single-chain URO-D crystals are isomorphous with wild-type uroporphyrinogen decarboxylase crystals | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
F217Y | recombinant mutant of the single chain of both modules substrate uroporphyrinogen-I, 2.5% of recombinant wild-type | Homo sapiens |
F217Y | recombinant mutant of the single chain of both modules substrate uroporphyrinogen-III, 14.5% of recombinant wild-type | Homo sapiens |
F217Y | recombinant mutant of the single chain of the first module substrate uroporphyrinogen-I, 41.3% of recombinant wild-type | Homo sapiens |
F217Y | recombinant mutant of the single chain of the first module substrate uroporphyrinogen-II, 50.9% of recombinant wild-type | Homo sapiens |
F217Y | recombinant mutant of the single chain of the second module substrate uroporphyrinogen-I, 46.2% of recombinant wild-type | Homo sapiens |
F217Y | recombinant mutant of the single chain of the second module substrate uroporphyrinogen-III, 52.7% of recombinant wild-type | Homo sapiens |
F217Y | recombinant mutant substrate uroporphyrinogen-I, 2.6% of recombinant wild-type | Homo sapiens |
additional information | construction of a single-chain protein (single-chain URO-D) in which the two subunits are connected by a flexible linker. The crystal structure of this protein is shown to be superimposable with wild-type activity and to have comparable catalytic activity | Homo sapiens |
additional information | variants of the linked dimer in which either of the active sites is inactivated by site-directed mutagenesis maintained approximately half of the wildtype catalytic activity, all four decarboxylations can be catalyzed at a single active site and shuttling of intermediates between active sites of the uroporphyrinogen decarboxylase dimer is not required | Homo sapiens |
Y164G | recombinant mutant of the single chain of the first module substrate uroporphyrinogen-I, 13.2% of recombinant wild-type | Homo sapiens |
Y164G | recombinant mutant substrate uroporphyrinogen-I, 8.1% of recombinant wild-type | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
42000 | - |
SDS-PAGE native URO-D protein | Homo sapiens |
84000 | - |
SDS-PAGE scURO-D-protein | Homo sapiens |
86000 | - |
analytical ultracentrifugation scURO-D | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
uroporphyrinogen-III | Homo sapiens | - |
coproporphyrinogen-III + 4 CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P06132 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
uroporphyrinogen-I | - |
Homo sapiens | coproporphyrinogen-I + 4 CO2 | - |
? | |
uroporphyrinogen-III | - |
Homo sapiens | coproporphyrinogen-III + 4 CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | SDS-PAGE, the dimeric structure of uroporphyrinogen decarboxylase is required to achieve conformational stability and to create a large active-site cleft | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
URO-D | - |
Homo sapiens |
uroporphyrinogen decarboxylase | - |
Homo sapiens |