Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1 | - |
L-aspartate | using O2 as electron acceptor | Bacillus subtilis | |
1.43 | - |
fumarate | - |
Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
monomer, gel filtration | Bacillus subtilis |
115000 | - |
dimer, gel filtration | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P38032 | - |
- |
Purification (Comment) | Organism |
---|---|
using NH4SO4 precipitation and using a DEAE-sepharose column | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + fumarate | - |
Bacillus subtilis | iminoaspartate + succinate | - |
? | |
L-aspartate + O2 | - |
Bacillus subtilis | iminoaspartate + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | gel filtration, 2 * 55000 Da, dimer in the absence of NaCl | Bacillus subtilis |
monomer | gel filtration, monomer in the presence of 150 mM NaCl | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
L-aspartate oxidase | - |
Bacillus subtilis |
nadB | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
L-aspartate | using O2 as electron acceptor | Bacillus subtilis | |
0.5 | - |
fumarate | - |
Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
physiological function | NadB and NadA (quinolinate synthase) interact with each other. The interaction is not species-specific and both proteins are not tightly bound to one another, indicating a function as a reversible multienzyme complex | Bacillus subtilis |
physiological function | NadB shows three enzymatic activities: L-aspartate-oxygen oxidoreductase activity, fumarate reductase activity, and L-aspartate-fumarate oxidoreductase activity | Bacillus subtilis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
L-aspartate | using O2 as electron acceptor | Bacillus subtilis | |
0.35 | - |
fumarate | - |
Bacillus subtilis |