CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.700 | Flavocytochrome C3; Chain A, domain 1 |
|
3.90.700.10 | Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain |
Domain Context
CATH Clusters
| Superfamily | Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain |
| Functional Family | L-aspartate oxidase |
Enzyme Information
| 1.4.3.16 |
L-aspartate oxidase.
based on mapping to UniProt P10902
L-aspartate + O(2) = iminosuccinate + H(2)O(2).
-!- L-aspartate oxidase catalyzes the first step in the de novo biosynthesis of NAD(+) in some bacteria. -!- O(2) can be replaced by fumarate as electron acceptor, yielding succinate. -!- The ability of the enzyme to use both O(2) and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions. -!- Iminosuccinate can either be hydrolyzed to form oxaloacetate and NH(3) or can be used by EC 2.5.1.72 in the production of quinolinate.
|
UniProtKB Entries (1)
| P10902 |
NADB_ECOLI
Escherichia coli K-12
L-aspartate oxidase
|
PDB Structure
| PDB | 1KNP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis.
Biochemistry
|
