EC Number | Application | Comment | Organism |
---|---|---|---|
1.4.1.21 | analysis | development of a genetically encoded fluorescent protein construct for monitoring of L-Asp in vitro, and employment of aspartate dehydrogenase scaffold as a biorecognition element | Thermotoga maritima |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.4.1.21 | expression of N-terminally His-tagged and GFP-tagged enzyme, using the flexible GGSGG linker, in Escherichia coli. The recombinant tagged aspartate dehydrogenase functions as the biorecognition element, and aspartate-induced conformational change is converted to a fluorescence signal by GFP, method, overview | Thermotoga maritima |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.1.21 | L-aspartate + H2O + NAD(P)+ | Thermotoga maritima | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.1.21 | Thermotoga maritima | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.4.1.21 | recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography | Thermotoga maritima |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.1.21 | L-aspartate + H2O + NAD(P)+ | - |
Thermotoga maritima | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
1.4.1.21 | additional information | high substrate specificity of aspartate dehydrogenase enzyme | Thermotoga maritima | ? | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.1.21 | NAD+ | - |
Thermotoga maritima | |
1.4.1.21 | NADH | - |
Thermotoga maritima | |
1.4.1.21 | NADP+ | - |
Thermotoga maritima | |
1.4.1.21 | NADPH | - |
Thermotoga maritima |