Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Synechocystis sp. |
Crystallization (Comment) | Organism |
---|---|
refined at 2.55 A resolution in complex with L-lysine and L-threonine | Synechocystis sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-lysine | enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-lysine, the enzyme displays partial inhibition by L-threonine (50% residual activity at saturation with L-threonine) with a K0.5 value of 0.7 mM | Synechocystis sp. | |
L-threonine | enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-threonine, the enzyme is inhibited by Lys in a cooperative manner, but the inhibition requires very high concentrations of L-lysine | Synechocystis sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
140000 | - |
gel filtration, homodimer | Synechocystis sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | P74569 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate | - |
Synechocystis sp. | ADP + 4-phospho-L-aspartate | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | crystal structure, dimerization involves only the catalytic domain | Synechocystis sp. |
Synonyms | Comment | Organism |
---|---|---|
AKbeta | - |
Synechocystis sp. |
AKsyn | - |
Synechocystis sp. |
aspartate kinase beta | - |
Synechocystis sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Synechocystis sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Synechocystis sp. |