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Literature summary for 6.3.5.2 extracted from

  • Patel, N.; Moyed, H.S.; Kane, J.F.
    Xanthosine-5'-phosphate amidotransferase from Escherichia coli (1975), J. Biol. Chem., 250, 2609-2613.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
6-diazo-5-oxo-L-norleucine Gln-dependent activity is more sensitive than NH4+-dependent activity; inhibition of Gln-dependent activity and NH4+-dependent activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
NH4+ Gln Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli B96
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + XMP + Gln identical Km value for NH4+ and Gln Escherichia coli AMP + diphosphate + GMP + Glu
-
?
ATP + XMP + Gln Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity Escherichia coli AMP + diphosphate + GMP + Glu
-
?
ATP + XMP + Gln identical Km value for NH4+ and Gln Escherichia coli B96 AMP + diphosphate + GMP + Glu
-
?
ATP + XMP + Gln Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity Escherichia coli B96 AMP + diphosphate + GMP + Glu
-
?
ATP + XMP + NH4+ identical Km value for NH4+ and Gln Escherichia coli AMP + diphosphate + GMP
-
?
ATP + XMP + NH4+ Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity Escherichia coli AMP + diphosphate + GMP
-
?
ATP + XMP + NH4+ identical Km value for NH4+ and Gln Escherichia coli B96 AMP + diphosphate + GMP
-
?
ATP + XMP + NH4+ Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity Escherichia coli B96 AMP + diphosphate + GMP
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
Gln-dependent activity and NH4+-dependent activity Escherichia coli