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Literature summary for 1.14.14.47 extracted from
- Substrate-ligand interactions in Geobacillus stearothermophilus nitric oxide synthase (2008), Biochemistry, 47, 12389-12397.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| enzyme exhibits two conformations in the absence of substrate. The addition of L-Arg stabilizes the conformer more similar to the Mus muculus enzyme, whereas N-hydroxy-L-arginine stabilizes the conformer more similar to the Bacillus subtilis enzyme, although both substrates introduce a positive electrostatic potential to the distal heme pocket | Geobacillus stearothermophilus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | in the substrate-free form, the Fe-Cys stretching mode is detected at 342.5 per cm, similar to that of Bacillus subtilis NOS. The binding of L-Arg and N-hydroxy-L-arginine brings about a small decrease and increase in the Fe-Cys stretching frequency, respectively | Geobacillus stearothermophilus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Geobacillus stearothermophilus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Geobacillus stearothermophilus |
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