Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.21 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)

Cloned (Comment) Organism
-
Gallus gallus

General Stability

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
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)

Purification (Comment) Organism
-
Gallus gallus

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
-
Gallus gallus 1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
?

Turnover Number [1/s]

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