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Literature summary extracted from

  • Firestine, S.M.; Davisson, V.J.
    Carboxylase in de novo purine biosynthesis. Characterization of the Gallus gallus bifunctional enzyme (1994), Biochemistry, 33, 11917-11926.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.21
-
Gallus gallus

General Stability

EC Number General Stability Organism
4.1.1.21 prolonged dialysis of more than 12 h, results in 50% loss of activity Gallus gallus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.21 0.076
-
1-(5-phosphoribosyl)-5-aminoimidazole
-
Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.21 Gallus gallus
-
bifunctional enzyme: phosphoribosylaminoimidazole carboxylase/4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide synthetase, with two independent folding domains, each containing a different catalytic site
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.21
-
Gallus gallus

Storage Stability

EC Number Storage Stability Organism
4.1.1.21 4°C, stable for at least 6 months Gallus gallus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.21 1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
-
Gallus gallus 1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.21 40
-
1-(5-phosphoribosyl)-5-aminoimidazole
-
Gallus gallus