Higher plants contain L-asparate oxidase, the first enzyme of the Escherichia coli quinolinate synthetase system.

Cotton callus cells contain an L-aspartate oxidase which does not appear to be active with D-aspartate, L-glutamate or D- or L-alanine. The enzyme requires for activity a dialyzable cofactor with an apparent molecular weight of 1,050. Since L-aspartate oxidase is the first enzyme of the pathway for de novo synthesis of the pyridine ring in Escherichia coli, this finding suggests that higher plants may use the L-aspartate-dihydroxyacetone phosphate pathway for de novo pyridine nucleotide biosynthesis.