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Literature summary for 2.5.1.61 extracted from

  • Miller, A.D.; Hart, G.J.; Packman, L.C.; Battersby, A.R.
    Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242 (1988), Biochem. J., 254, 915-918.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
porphobilinogen Escherichia coli
-
 ?
-
 ?
porphobilinogen Escherichia coli TG1
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 TG1
-
Escherichia coli TG1
-
 TG1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 porphobilinogen in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75 Escherichia coli uroporphyrinogen III + 4 NH3
-
 ?
4 porphobilinogen in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75 Escherichia coli TG1 uroporphyrinogen III + 4 NH3
-
 ?
4 porphobilinogen + H2O
-
 Escherichia coli hydroxylmethylbilane + 4 NH3
-
 ?
4 porphobilinogen + H2O
-
 Escherichia coli TG1 hydroxylmethylbilane + 4 NH3
-
 ?
porphobilinogen
-
 Escherichia coli ?
-
 ?
porphobilinogen
-
 Escherichia coli TG1 ?
-
 ?