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 | 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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Oxidation Stability | Organism |
---|---|
anaerobic conditions stabilize | Bacillus subtilis |
oxygen-labile in vivo and in vitro, AMP protects | Bacillus subtilis |
Purification (Comment) | Organism |
---|---|
protamine sulfate, DEAE-cellulose | Bacillus subtilis |
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 | Comment | Organism |
---|---|---|
? | 2-4 * 50000, SDS-PAGE | Bacillus subtilis |