Cloned (Comment) | Organism |
---|---|
both catalytic domains of the enzyme, performing each one of the enzyme activities, are expressed separately with or without the interface region, resulting in increased activity of each domain compared to the wild-type bifunctional holoenzyme, the isolated catalytic domains are no longer allosterically regulated, expression of hybrid holoenzyme AKIII-HDHI+ | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-threonine | feedback inhibition | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.51 | - |
L-aspartate | recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity | Escherichia coli | |
0.63 | - |
L-aspartate | recombinant wild-type bifunctional holoenzyme, asparate kinase activity | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate | Escherichia coli | part of the aspartate pathway of amino acid biosynthesis | ADP + 4-phospho-L-aspartate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate | part of the aspartate pathway of amino acid biosynthesis | Escherichia coli | ADP + 4-phospho-L-aspartate | - |
? | |
ATP + L-aspartate | aspartate kinase activity | Escherichia coli | ADP + 4-phospho-L-aspartate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.16 | - |
L-aspartate | recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity | Escherichia coli | |
0.39 | - |
L-aspartate | recombinant wild-type bifunctional holoenzyme, asparate kinase activity | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.33 | - |
L-threonine | recombinant wild-type bifunctional holoenzyme, inhibition of asparate kinase activity | Escherichia coli |