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Literature summary for 2.5.1.61 extracted from

  • Haedener, A.; Alefounder, P.; Hart, G.J.; Abell, C.; Battersby, A.R.
    Investigation of putative active-site lysine residues in C (1990), Biochem. J., 271, 487-491.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
K55Q K55Q mutant Escherichia coli
K55Q/K59Q K55Q-K59Q mutant, lower specific activity than the wild-type enzyme Escherichia coli
K59Q K59Q mutant, lower specific activity than the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NaBH4 partially inactivates Escherichia coli
pyridoxal 5'-phosphate partially inactivates 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
-
 wild-type TG' recO, mutants K55Q, K59Q, and K55Q-K59Q
-

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 ?
-
 ?

Synonyms

Synonyms Comment Organism
porphobilinogen deaminase
-
 Escherichia coli