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Literature summary for 2.4.2.14 extracted from

  • Liras, A.; Argomaniz, L.; Llorente, P.
    Presence, preliminary properties and partial purification of 5-phosphoribosylpyrophosphate amidotransferase from Artemia sp (1990), Biochim. Biophys. Acta, 1033, 114-117.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
5',5'-P1,P4-diguanosine tetraphosphate IC50: 0.4 mM, 2 mM, approx. 80% inhibition Artemia sp.
ADP 1 mM, approx. 95% inhibition Artemia sp.
AMP 1 mM, approx. 40% inhibition Artemia sp.
GDP 1 mM, approx. 75% inhibition Artemia sp.
GMP 1 mM, approx. 60% inhibition Artemia sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
5-phospho-alpha-D-ribose 1-diphosphate cosubstrate NH3 Artemia sp.
0.7
-
5-phospho-alpha-D-ribose 1-diphosphate cosubstrate glutamine Artemia sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Artemia sp.
-
-

Organism

Organism UniProt Comment Textmining
Artemia sp.
-
brine shrimp, activity increases 7fold during early larval development in 2 d old Artemia
-

Purification (Commentary)

Purification (Comment) Organism
partial Artemia sp.

Source Tissue

Source Tissue Comment Organism Textmining
nauplius
-
Artemia sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
Artemia sp. 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
ir
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O lower aminotransferase activity compared to amidotransferase activity Artemia sp. 5-phospho-beta-D-ribosylamine + diphosphate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Artemia sp.

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.4
-
IC50: 0.4 mM, 2 mM, approx. 80% inhibition Artemia sp. 5',5'-P1,P4-diguanosine tetraphosphate