Literature summary for 2.4.2.14 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.

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General Stability

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe	iron is oxidized by O2 to enzyme-bound Fe3+	Bacillus subtilis
Fe	enzyme contains a [4Fe-4S] cluster	Bacillus subtilis
additional information	4Fe-4S-cluster	Bacillus subtilis
additional information	S2- is oxidized by O2 to a mixture of sulfur oxides bound as thiocysteine and yet unidentified products	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Oxidation Stability

Oxidation Stability	Organism
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)

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	-	?

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Release 2023.1 (January 2023)