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Literature summary for 2.4.2.14 extracted from

  • Wong, J.Y.; Bernlohr, D.A.; Turnbough, C.L.; Switzer, R.L.
    Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis (1981), Biochemistry, 20, 5669-5674.
    View publication on PubMed

General Stability

General Stability Organism
ADP or ADP and GMP, ratio 1/1, stabilize equilibrium between dimeric and tetrameric form Bacillus subtilis
AMP or GMP stabilizes dimeric enzyme form Bacillus subtilis
AMP stabilizes against inactivation by O2 Bacillus subtilis
GDP stabilizes tetrameric enzyme form Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe iron-sulfur center can be removed with 1,10-phenanthroline, resulting apoprotein is devoid of amino- and amidotransferase activity Bacillus subtilis
Fe required, iron-sulfur protein Bacillus subtilis
Fe enzyme contains a [4Fe-4S] cluster Bacillus subtilis
additional information 4Fe-4S-cluster Bacillus subtilis
additional information sulfur required, iron-sulfur protein Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
2-4 * 50000, SDS-PAGE Bacillus subtilis
93000
-
sucrose density gradient centrifugation, enzyme exists in equilibrium of tetrameric, dimeric and monomeric forms Bacillus subtilis
185000
-
highly concentrated enzyme solution, sucrose density gradient centrifugation, enzyme exists in equilibrium of tetramer, dimer and monomeric forms, conversion of dimer to tetramer within 10fold increase in protein concentration Bacillus subtilis
200000
-
highly concentrated enzyme solution, gel filtration, enzyme exists in equilibrium of tetrameric, dimeric and monomeric forms, conversion of dimer to tetramer within 10fold increase in protein concentration, AMP and GMP stabilize the dimeric form, GDP stabilizes the tetrameric form Bacillus subtilis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Oxidation Stability

Oxidation Stability Organism
anaerobic conditions stabilize Bacillus subtilis
oxygen-labile in vivo and in vitro, AMP protects Bacillus subtilis

Purification (Commentary)

Purification (Comment) Organism
protamine sulfate, DEAE-cellulose Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
Bacillus subtilis 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Bacillus subtilis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
?

Subunits

Subunits Comment Organism
? 2-4 * 50000, SDS-PAGE Bacillus subtilis