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L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.
The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.
Synthesis of quinolinate from D-aspartate in the mammalian liver-Escherichia coli quinolinate synthetase system.
The mode of condensation of aspartic acid and dihydroxyacetone phosphate in quinolinate synthesis in Escherichia coli.
Evidence for an intermediate in quinolinate biosynthesis in Escherichia coli
Results of these experiments indicate that the nadB gene product forms an unstable compound from aspartate in the presence of flavine adenine dinucleotide, and that this compound is then condensed with dihydroxyacetone phosphate to form quinolinate in a reaction catalyzed by the n adA gene product.
Occurrence in mammalian liver of a protein which replaces the B protein of E. coli quinolinate synthetase.