Crystallization (Comment) | Organism |
---|---|
structure of isoform IGPD2 in complex with phosphate, to 1.75 A resolution. The holoenzyme has an open conformation where the C-terminal region (R193-R206, termed the C loop), which contains a number of conserved residues, is disordered. structure of mutant E21Q, to 1.12 A resolution | Arabidopsis thaliana |
Protein Variants | Comment | Organism |
---|---|---|
E21Q | mutation in putative acid-base catalyst, inactive | Arabidopsis thaliana |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
phosphate | - |
Arabidopsis thaliana |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Arabidopsis thaliana | 9507 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | O23346 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | mechanism shows an enzyme-catalyzed formation of a high-energy imidazolate intermediate. Changes in manganese coordination chemistry dominate all aspects of catalysis. In the first part of the reaction, the enzyme harnesses the substrate binding energy to create a distorted, ligand-depleted metal center, which serves to remove kinetic barriers to the production of the imidazolate intermediate. Subsequently, a second switch in coordination chemistry restores the octahedral coordination of the metal ion, leading to critical torsion angle changes to the substrate that are necessary for concomitant production of the diazafulvene | Arabidopsis thaliana | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HisN5B | - |
Arabidopsis thaliana |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
5 | - |
phosphate | 30°C, pH not specified in the publication | Arabidopsis thaliana |