Literature summary for 4.1.1.37 extracted from

Phillips, J.D.; Whitby, F.G.; Kushner, J.P.; Hill, C.P.
Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase (2003), EMBO J., 22, 6225-6233.

Search for more literature for 4.1.1.37

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21-pLysS	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallized in complex with coproporphyrinogen by sitting drop vapor diffusion, crystals belong to space group P3(1)21, unit cell dimensions a : b :102.9 A, c : 74.5 A	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D86	site-directed mutagenesis	Homo sapiens
D86E	site-directed mutagenesis	Homo sapiens
D86G	site-directed mutagenesis	Homo sapiens
Y164F	site-directed mutagenesis	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Uroporphyrinogen III	Homo sapiens	tetrapyrrole coordination, fifth step in the heme biosynthetic pathway	Coproporphyrinogen III + 4 CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P06132	human	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Uroporphyrinogen III	-	Homo sapiens	Coproporphyrinogen III + 4 CO2	-	?
Uroporphyrinogen III	tetrapyrrole coordination, fifth step in the heme biosynthetic pathway	Homo sapiens	Coproporphyrinogen III + 4 CO2	-	?

Synonyms

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

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Release 2023.1 (January 2023)