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

BRENDA support

Literature summary extracted from

  • Bernlohr, D.A.; Switzer, R.L.
    Reaction of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase with oxygen: chemistry and regulation by ligands (1981), Biochemistry, 20, 5675-5681.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.4.2.14 AMP stabilizes against inactivation by O2 Bacillus subtilis
2.4.2.14 phosphoribosyldiphosphate and other nucleotides antagonize stabilizing effect of AMP Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.14 Fe iron is oxidized by O2 to enzyme-bound Fe3+ 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 S2- is oxidized by O2 to a mixture of sulfur oxides bound as thiocysteine and yet unidentified products Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.14 Bacillus subtilis
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
2.4.2.14 O2, rather than peroxide, superoxide, hydroxyl radical or singlet oxygen, inactivates, allosteric inhibitors, such as AMP, ADP, GMP or GDP modulate the rate of inactivation 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
-
 ?