Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
expression in Escherichia coli | Bacillus subtilis |
General Stability | Organism |
---|---|
AMP or GMP stabilizes dimeric enzyme form | Bacillus subtilis |
GDP stabilizes tetrameric enzyme form | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.072 | - |
5-phospho-alpha-D-ribose 1-diphosphate | - |
Bacillus subtilis | |
4.3 | - |
L-glutamine | - |
Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | enzyme contains a diamagnetic [4Fe-4S] cluster essential for activity | Bacillus subtilis | |
additional information | - |
Gallus gallus | |
additional information | non-heme iron is not present in significant amounts | Escherichia coli | |
additional information | probably diamagnetic | Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Gallus gallus |
50000 | - |
2-4 * 50000, SDS-PAGE | Bacillus subtilis |
56395 | - |
3-4 * 56395, calculated from nucleotide sequence | Escherichia coli |
57000 | - |
3-4 * 57000, SDS-PAGE | Escherichia coli |
194000 | - |
sedimentation equilibrium centrifugation | Escherichia coli |
224000 | - |
gel filtration | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Escherichia coli | - |
- |
- |
Gallus gallus | - |
- |
- |
Oxidation Stability | Organism |
---|---|
in vitro O2 oxidizes iron in the Fe-S cluster to the high spin ferric state and sulfur to a mixtur of S in thiocystine residues plus other unidentified products | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | mechanism of glutamine amide transfer | Bacillus subtilis | |
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | mechanism of glutamine amide transfer | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.043 | - |
- |
Bacillus subtilis |
17.2 | - |
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | - |
Gallus gallus | 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate | - |
? | |
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | - |
Escherichia coli | 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate | - |
? | |
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | reaction at 70% the rate of aminotransferase activity | Bacillus subtilis | 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate | - |
? | |
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | - |
Gallus gallus | 5-phospho-beta-D-ribosylamine + diphosphate | - |
? | |
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | no activity with NH4+ | Bacillus subtilis | 5-phospho-beta-D-ribosylamine + diphosphate | - |
? | |
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O | no activity with NH4+ | Escherichia coli | 5-phospho-beta-D-ribosylamine + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | - |
Gallus gallus |
? | 2-4 * 50000, SDS-PAGE | Bacillus subtilis |
? | 3-4 * 56395, calculated from nucleotide sequence | Escherichia coli |
? | 3-4 * 57000, SDS-PAGE | Escherichia coli |