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Literature summary for 4.2.1.75 extracted from

  • Schubert, H.L.; Raux, E.; Matthews, M.A.; Phillips, J.D.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
    Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase (2002), Biochem. Soc. Trans., 30, 595-600.
    View publication on PubMed
Search for more literature for 4.2.1.75

Protein Variants

Protein Variants Comment Organism
additional information 16 known mutations causing congenital erythropoietic porphyria in humans via alterations of the tertiary enzyme structure Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 about Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hydroxymethylbilane Homo sapiens macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview uroporphyrinogen-III + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
hydroxymethylbilane = uroporphyrinogen III + H2O in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydroxymethylbilane linear tetrapyrrole Homo sapiens uroporphyrinogen-III + H2O
-
 ?
hydroxymethylbilane macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview Homo sapiens uroporphyrinogen-III + H2O
-
 ?

Subunits

Subunits Comment Organism
More enzyme structure, model Homo sapiens

Synonyms

Synonyms Comment Organism
U3S
-
 Homo sapiens
Uroporphyrinogen III synthase
-
 Homo sapiens