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Literature summary for 5.4.99.18 extracted from
- Multiple active site histidine protonation states in Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase detected by REDOR NMR (2007), Biochemistry, 46, 9507-9512.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| multiple REDOR NMR studies of a 151000 Da complex of uniformly 15N-labeled enzyme and the active site ligand [6-13C]-citrate show a single ionization equilibrium associated with the key histidine H59. H59 exists in approximately equimolar amounts of an Ndelta-unprotonated pyridine-like form and an Ndelta-protonated pyrrole-like form. Proton transfer mechanism involves H59 Ndelta | Acetobacter aceti |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acetobacter aceti | Q2QJL3 | - |
- |
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Release 2023.1 (January 2023)
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