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Literature summary extracted from
- Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure (2015), J. Biol. Inorg. Chem., 20, 757-770.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.99.48 | an optical spectroscopic and density functional theory characterization of azide- and cyanide-inhibited wild type and N7A IsdG. Residue Asn7 perturbs the electronic structure of azide-inhibited, but not cyanide-inhibited, IsdG. The terminal amide of Asn7 is a hydrogen bond donor to the alpha-atom of a distal ligand to heme in IsdG. The Asn7-N3 hydrogen bond influences the orientation of a distal azide ligand with respect to the heme substrate. Asn7-N3 hydrogen bond donation causes the azide ligand to rotate about an axis perpendicular to the porphyrin plane and weakens the pi-donor strength of the azide ligand | Staphylococcus aureus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.99.48 | azide | - |
Staphylococcus aureus |  |
| 1.14.99.48 | cyanide | - |
Staphylococcus aureus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.99.48 | Staphylococcus aureus | Q8NX62 | - |
- |
| 1.14.99.48 | Staphylococcus aureus MW2 | Q8NX62 | - |
- |
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