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Literature summary extracted from

  • Messenger, L.J.; Zalkin, H.
    Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties (1979), J. Biol. Chem., 254, 3382-3392.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.2.14 Mg-phosphoribosyldiphosphate no glutamine-binding site in the absence of Mg-phosphoribosyldiphosphate Escherichia coli
2.4.2.14 phosphoribosyl-5-phosphate 3-4fold activation of glutaminase activity in the presence of phosphate or diphosphate Escherichia coli

General Stability

EC Number General Stability Organism
2.4.2.14 stable during all stages of purification provided thiols and oxygen are avoided Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.14 2-amino-4-oxo-5-chloropentanoate approx. 80% inactivation of NH3-dependent activity after 30 min Escherichia coli
2.4.2.14 6-diazo-5-oxo-L-norleucine approx. 98% inactivation of amidotransferase activity after 30 min Escherichia coli
2.4.2.14 ADP
-
 Escherichia coli
2.4.2.14 AMP approx. 10 mM, complete inhibition, sigmoidal inhibition curve, competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate, GMP and AMP together have a synergistic effect on inhibition Escherichia coli
2.4.2.14 GDP
-
 Escherichia coli
2.4.2.14 GMP approx. 2.5 mM, complete inhibition, highly sigmoidal inhibition curve, competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate, GMP and AMP together have an synergistic effect on inhibition Escherichia coli
2.4.2.14 GTP 5 mM, 79% inhibition Escherichia coli
2.4.2.14 IMP 5 mM, 86% inhibition Escherichia coli
2.4.2.14 iodoacetamide approx. 60% inactivation of amidotransferase activity after 30 min, very weak inactivation of NH3-dependent activity Escherichia coli
2.4.2.14 p-mercuribenzoate 0.001 mM, complete inhibition Escherichia coli
2.4.2.14 XMP 51% inhibition; 5 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.14 0.067
-
 5-phospho-alpha-D-ribose 1-diphosphate
-
 Escherichia coli
2.4.2.14 1.7
-
 L-glutamine
-
 Escherichia coli
2.4.2.14 8.8
-
 NH3
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.14 Mg2+
-
 Escherichia coli
2.4.2.14 additional information non-heme iron is not present in significant amounts Escherichia coli
2.4.2.14 additional information not activated by iron or sulfide Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.14 57000
-
 3-4 * 57000, SDS-PAGE Escherichia coli
2.4.2.14 194000
-
 sedimentation equilibrium centrifugation Escherichia coli
2.4.2.14 224000
-
 gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Escherichia coli first reaction in de-novo pathway of purine biosynthesis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.14 Escherichia coli
-
 strains K-12 or B-96, purine requiring strain
-

Oxidation Stability

EC Number Oxidation Stability Organism
2.4.2.14 anaerobic conditions stabilize Escherichia coli
2.4.2.14 low concentrations of thiols e.g. dithiothreitol or 2-mercaptoethanol accelerate aerobic inactivation Escherichia coli
2.4.2.14 oxygen inactivates during purification Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.14 ammonium sulfate, heat treatment, DEAE-Sepharose, Blue Dextran-Sepharose, hydroxylapatite Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.14 17.2
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Escherichia coli 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Escherichia coli L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + H2O enzyme exhibits glutaminase activity in the absence of other substrates or effectors Escherichia coli L-glutamate + NH3
-
 ?
2.4.2.14 NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O 2.8fold higher aminotransferase activity compared to amidotransferase activity Escherichia coli 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.14 ? 3-4 * 57000, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.14 37
-
 assay at Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.2.14 additional information
-
 AMP and GMP enhance thermal stability Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.14 6.6 7.7 broad, amidotransferase activity, phosphate buffer Escherichia coli
2.4.2.14 7.8 8.6 broad, amidotransferase activity, Tris/HCl buffer Escherichia coli
2.4.2.14 8.5
-
 aminotransferase activity, Tris buffer Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.2.14 0.36
-
 AMP
-
 Escherichia coli