Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli BL21(DE3) | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + O2 | Escherichia coli | the first enzyme in the de novo synthesis of NAD+ in bacteria | iminosuccinate + H2O2 | - |
? | |
L-aspartate + O2 | Escherichia coli K12 | the first enzyme in the de novo synthesis of NAD+ in bacteria | iminosuccinate + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli K12 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + H2O + fumarate | can use either molecular oxygen or fumarate to reoxidize the reduced enzyme | Escherichia coli | oxaloacetate + NH3 + succinate | - |
? | |
L-aspartate + H2O + fumarate | can use either molecular oxygen or fumarate to reoxidize the reduced enzyme | Escherichia coli K12 | oxaloacetate + NH3 + succinate | - |
? | |
L-aspartate + O2 | the first enzyme in the de novo synthesis of NAD+ in bacteria | Escherichia coli | iminosuccinate + H2O2 | - |
? | |
L-aspartate + O2 | can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine | Escherichia coli | iminosuccinate + H2O2 | - |
? | |
L-aspartate + O2 | the first enzyme in the de novo synthesis of NAD+ in bacteria | Escherichia coli K12 | iminosuccinate + H2O2 | - |
? | |
L-aspartate + O2 | can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine | Escherichia coli K12 | iminosuccinate + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
L-aspartate oxidase | - |
Escherichia coli |
nadB | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | FAD-dependent enzyme | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate | Escherichia coli |
metabolism | the first enzyme in the de novo synthesis of NAD+ in bacteria | Escherichia coli |