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.
D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D003067:Coenzymes / Q000032:analysis; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*
D003067:Coenzymes; D029968:Escherichia coli Proteins; D009097:Multienzyme Complexes; C022512:quinolinic acid synthetase; D000594:Amino Acid Oxidoreductases; C031955:L-aspartate oxidase, E coli