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Literature summary for 4.1.1.37 extracted from

  • Phillips, J.D.; Parker, T.L.; Schubert, H.L.; Whitby, F.G.; Hill, C.P.; Kushner, J.P.
    Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase (2001), Blood, 98, 3179-3185.
    View publication on PubMed

Application

Application Comment Organism
medicine subnormal activity of uroporphyrinogen decarboxylase in hepatocytes is responsible for the most common form of porphyria in humans, porphyria cutanea tarda Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
cloned, sequenced and expressed in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant URO-D proteins G156D, F232L, and I260T 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 human
-

Purification (Commentary)

Purification (Comment) Organism
mutant URO-D proteins G156D, F232L, and I260T Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Uroporphyrinogen III
-
Homo sapiens Coproporphyrinogen III + 4 CO2
-
?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
additional information enzyme does not require cofactors or prosthetic groups for activity Homo sapiens