Crystallization (Comment) | Organism |
---|---|
catalytically inactive mutant C82A in complex with citric acid, 2.0 A resolution. Citric acid binds to the catalytic site, which induces a conformational change to close the active site. Residue R48 is responsible for recognizing carboxyl groups of the substrates L-/D-aspartates and stabilizing a reaction intermediate, and L164 is responsible for stabilizing a closed state structure | Pyrococcus horikoshii |
Protein Variants | Comment | Organism |
---|---|---|
C82A | catalytically inactive. Crystallization data in complex with citric acid | Pyrococcus horikoshii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Citric acid | competitive | Pyrococcus horikoshii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.7 | - |
L-aspartate | pH 8.0, 70°C | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O58403 | strain OT3 | - |
Pyrococcus horikoshii OT-3 | O58403 | strain OT3 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-aspartate = D-aspartate | one-base mechanism, residue C194 plays the role of the base for not only L-aspartate but also D-aspartate | Pyrococcus horikoshii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | - |
Pyrococcus horikoshii | D-aspartate | - |
? | |
L-aspartate | - |
Pyrococcus horikoshii OT-3 | D-aspartate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PhAspR | - |
Pyrococcus horikoshii |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
7.4 | - |
Citric acid | pH 8.0, 70°C | Pyrococcus horikoshii |