EC Number   |
General Information |
Reference |
|---|
    1.4.3.16 | 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 |
-, 764137 |
| 1.4.3.16 | malfunction |
although the enzyme mutation dramatically affects NADPH oxidase RBOHD function, it does not affect functions carried out by other members of the RBOH family, such as RBOHC and RBOHF |
726225 |
| 1.4.3.16 | metabolism |
the enzyme catalyzes the first irreversible step in the de novo biosynthesis of NAD+ |
726225 |
| 1.4.3.16 | metabolism |
the first enzyme in the de novo synthesis of NAD+ in bacteria |
-, 764137 |
| 1.4.3.16 | more |
full enzyme activity is not required for flg22-induced responses that are NADPH oxidase RBOHD-independent |
726225 |
| 1.4.3.16 | more |
LASPO displays strong primary and tertiary structure similarity with the flavin containing subunit of the proteins belonging to the succinate dehydrogenase/fumarate reductase family. The similarity extends to the active site residues, with LASPO differing from the other enzymes of the family only for the presence of a conserved glutamate 121, which is substituted by apolar amino acids in the other enzymes |
711324 |
| 1.4.3.16 | physiological function |
LASPO is a flavoenzyme catalyzing the first step in the de novo biosynthesis of NAD+. The enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor |
711324 |
| 1.4.3.16 | 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 |
686712 |
| 1.4.3.16 | physiological function |
NadB shows three enzymatic activities: L-aspartate-oxygen oxidoreductase activity, fumarate reductase activity, and L-aspartate-fumarate oxidoreductase activity |
686712 |
| 1.4.3.16 | physiological function |
the enzyme catalyzes a key metabolic step for the production of the nucleotide cofactor NAD+ |
765612 |
