1.4.3.16 3-hydroxy-erythro-L-aspartate + O2 - Escherichia coli 2-amino-3-hydroxy-2-butenedioic acid + H2O2 - ? 414038 1.4.3.16 DL-aspartate + O2 - Sulfurisphaera tokodaii iminosuccinate + H2O2 - ? 441340 1.4.3.16 L-asparagine + H2O + O2 - Sulfurisphaera tokodaii 4-amino-2,4-dioxobutanoate + NH3 + H2O2 - ? 424849 1.4.3.16 L-asparagine + H2O + O2 low activity Pseudomonas putida 4-amino-2,4-dioxobutanoate + NH3 + H2O2 - ? 424849 1.4.3.16 L-asparagine + O2 Vmax/Km is 63fold lower compared to L-aspartate Sulfurisphaera tokodaii 4-amino-2-imino-4-oxobutanoate + H2O2 - ? 423725 1.4.3.16 L-aspartate + fumarate - Bacillus subtilis iminoaspartate + succinate - ? 460031 1.4.3.16 L-aspartate + fumarate - Escherichia coli iminosuccinate + succinate - ? 413426 1.4.3.16 L-aspartate + H2O + fumarate - Escherichia coli oxaloacetate + NH3 + succinate - ? 371006 1.4.3.16 L-aspartate + H2O + fumarate - Arabidopsis thaliana oxaloacetate + NH3 + succinate - ? 371006 1.4.3.16 L-aspartate + H2O + fumarate it is very likely, that fumarate and not O2 is the physiological electron acceptor in vivo Escherichia coli oxaloacetate + NH3 + succinate - ? 371006 1.4.3.16 L-aspartate + H2O + fumarate can use either molecular oxygen or fumarate to reoxidize the reduced enzyme Escherichia coli oxaloacetate + NH3 + succinate - ? 371006 1.4.3.16 L-aspartate + H2O + fumarate can use either molecular oxygen or fumarate to reoxidize the reduced enzyme Escherichia coli K12 oxaloacetate + NH3 + succinate - ? 371006 1.4.3.16 L-aspartate + H2O + O2 - Escherichia coli oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 - Arabidopsis thaliana oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 - Gossypium hirsutum oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 - Sulfurisphaera tokodaii oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 best substrate Pseudomonas putida oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 specific for L-aspartate Escherichia coli oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 2,6-dichlorophenol-indophenol, ferricyanide and fumarate can be electron acceptor Pyrococcus horikoshii oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 fumarate or succinate can be electron acceptor instead of O2 Escherichia coli oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 first enzyme of quinolinate synthetase system Escherichia coli oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 oxidation is accelerated in the presence of 0.5 mM fumarate, fumarate appears to be the preferred electron acceptor since its presence inhibits oxygen reduction by 90% Escherichia coli oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate Sulfurisphaera tokodaii oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + H2O + O2 2,6-dichlorophenol-indophenol, ferricyanide and fumarate can be electron acceptor Pyrococcus horikoshii OT-3 oxaloacetate + NH3 + H2O2 - ? 258998 1.4.3.16 L-aspartate + O2 - Bacillus subtilis iminoaspartate + H2O2 - ? 409635 1.4.3.16 L-aspartate + O2 - Escherichia coli iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 - Arabidopsis thaliana iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 - Sulfurisphaera tokodaii iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 - Thermococcus litoralis iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate Sulfurisphaera tokodaii iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 first enzyme of the de novo biosynthetic pathway of NAD+ in plants Arabidopsis thaliana iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 the first enzyme in the de novo synthesis of NAD+ in bacteria Escherichia coli iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine Escherichia coli iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 highly specific for L-aspartate and does not act on other natural amino acids Thermococcus litoralis iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 - Thermococcus litoralis DSM 5473 iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 highly specific for L-aspartate and does not act on other natural amino acids Thermococcus litoralis DSM 5473 iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 the first enzyme in the de novo synthesis of NAD+ in bacteria Escherichia coli K12 iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine Escherichia coli K12 iminosuccinate + H2O2 - ? 413427 1.4.3.16 L-aspartate + O2 - Arabidopsis thaliana alpha-iminosuccinate + H2O2 - ? 424851 1.4.3.16 L-glutamate + H2O + O2 low activity Pseudomonas putida 2-oxopentanedioate + NH3 + H2O2 - ? 424854 1.4.3.16 additional information the enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor. No activity with 3-hydroxy-threo-L-aspartate Escherichia coli ? - ? 89 1.4.3.16 additional information the enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor. Catalytic role of the active site residue E121, substrate specificity of wild-type and mutant enzymes, molecular docking studies, role of R290, overview. E121 interacts favourably with the charged amino group of the substrate and different ligands might assume different orientations in the active site of the enzyme, binding modes for L-aspartate, overview Escherichia coli ? - ? 89 1.4.3.16 additional information the enzyme does not show activity on L-phenylalanine (50–100 mM), L-glutamate (50–100 mM), glycine (50–100 mM), L-proline (50–100 mM) and L-alanine (50–100 mM) Sulfurisphaera tokodaii ? - ? 89 1.4.3.16 additional information the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine Sulfurisphaera tokodaii ? - ? 89 1.4.3.16 N-acetyl-L-aspartate + O2 - Escherichia coli ? + H2O2 - ? 414913 1.4.3.16 N-formyl-L-aspartate + O2 - Escherichia coli ? + H2O2 - ? 414951