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

BRENDA support

Literature summary 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

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.14 50000
-
 2-4 * 50000, SDS-PAGE Bacillus subtilis
2.4.2.14 93000
-
 sucrose density gradient centrifugation, enzyme exists in equilibrium of tetrameric, dimeric and monomeric forms Bacillus subtilis
2.4.2.14 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
2.4.2.14 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)

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 Bacillus subtilis 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 Bacillus subtilis
-
-
-

Oxidation Stability

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

Purification (Commentary)

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

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
-
 Bacillus subtilis 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 Bacillus subtilis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.14 ? 2-4 * 50000, SDS-PAGE Bacillus subtilis