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Literature summary for 4.1.1.37 extracted from

  • Phillips, J.D.; Warby, C.A.; Whitby, F.G.; Kushner, J.P.; Hill, C.P.
    Substrate shuttling between active sites of uroporphyrinogen decarboxylase is not required to generate coproporphyrinogen (2009), J. Mol. Biol., 389, 306-314.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli as His-tagged enzyme Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
modified enzyme single-chain URO-D crystals are isomorphous with wild-type uroporphyrinogen decarboxylase crystals Homo sapiens

Protein Variants

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 [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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
uroporphyrinogen-III Homo sapiens
-
coproporphyrinogen-III + 4 CO2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P06132
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
URO-D
-
Homo sapiens
uroporphyrinogen decarboxylase
-
Homo sapiens