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Literature summary extracted from

  • Silva, P.J.; Ramos, M.J.
    Comparative density functional study of models for the reaction mechanism of uroporphyrinogen III synthase (2008), J. Phys. Chem. B, 112, 3144-3148.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.75 hydroxymethylbilane Homo sapiens the D-ring of the hydroxymethylbilane substrate binds to the enzyme in a conformation that shields its terminal portion from reacting with ring A and prevents the formation of the biologically useless uroporphyrinogen I, reaction mechanism, overview uroporphyrinogen III + H2O
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Organism

EC Number Organism UniProt Comment Textmining
4.2.1.75 Homo sapiens P10746
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Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.75 hydroxymethylbilane = uroporphyrinogen III + H2O reaction mechanism, modelling, overview Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.75 hydroxymethylbilane the D-ring of the hydroxymethylbilane substrate binds to the enzyme in a conformation that shields its terminal portion from reacting with ring A and prevents the formation of the biologically useless uroporphyrinogen I, reaction mechanism, overview Homo sapiens uroporphyrinogen III + H2O
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4.2.1.75 hydroxymethylbilane the enzyme catalyzes the inversion of one of the four heterocyclic rings present in the substrate. Reaction mechanism analysis by high-level quantum mechanical calculations on model systems of the enzyme Homo sapiens uroporphyrinogen III + H2O
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Synonyms

EC Number Synonyms Comment Organism
4.2.1.75 Uroporphyrinogen III synthase
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Homo sapiens