PMID:7049247
| Citation |
Nasu, S, Wicks, FD and Gholson, RK (1982) The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase. Biochim. Biophys. Acta 704:240-52 |
|---|---|
| Abstract |
In Escherichia coli quinolinic acid, a precursor of NAD+, is synthesized from L-aspartate and dihydroxyacetone phosphate by two enzymes, an FAD-containing 'B protein' and 'A protein'. An enzyme which can replace the B protein in the E. coli quinolinate synthetase system when D-aspartate replaces L-aspartate as a substrate has been purified 300-fold from bovine kidney. This enzyme is shown to be identical with the previously described D-aspartate oxidase (D-aspartate:oxygen oxidoreductase (deaminating), EC 1.4.3.1). The immediate reaction product of D-aspartate oxidase (iminoaspartate) is condensed with dihydroxyacetone phosphate to form quinolinate in a reaction catalyzed by E. coli quinolinate synthetase A protein. In the absence of A protein (or dihydroxyacetone phosphate) iminoaspartate is spontaneously hydrolyzed to form oxaloacetate with a half-life of about 2.5 min at 25 degrees C and pH 8.0. |
| Links | |
| Keywords |
Amino Acid Oxidoreductases/isolation & purification; Amino Acid Oxidoreductases/metabolism; Animals; Cattle; D-Aspartate Oxidase; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Kidney/enzymology; Liver/enzymology; Macromolecular Substances; Molecular Weight; Multienzyme Complexes/metabolism; Rats; Temperature |
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