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Literature summary for 2.5.1.61 extracted from

  • Hart, G.J.; Abell, C.; Battersby, A.R.
    Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli (1986), Biochem. J., 240, 273-276.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.61

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39100
-
 1 * 39100, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K12, JA 200/pLC 41-4
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

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 + H2O
-
 Escherichia coli hydroxylmethylbilane + 4 NH3
-
 ?
porphobilinogen
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 39100, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
porphobilinogen deaminase
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
-
 Escherichia coli