EC - L-aspartate oxidase

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IntEnz Enzyme Nomenclature


Accepted name:
L-aspartate oxidase
Other names:
Systematic name:
L-aspartate:oxygen oxidoreductase (deaminating)




A flavoprotein (FAD). L-Aspartate oxidase catalyses the first step in the de novo biosynthesis of NAD+ in some bacteria. O2 can be replaced by fumarate as electron acceptor, yielding succinate [5]. The ability of the enzyme to use both O2 and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions [5]. Iminosuccinate can either be hydrolysed to form oxaloacetate and NH3 or can be used by EC, quinolinate synthase, in the production of quinolinate. The enzyme is a member of the succinate dehydrogenase/fumarate-reductase family of enzymes [5].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008734 , GO:0044318
CAS Registry Number: 69106-47-4
UniProtKB/Swiss-Prot: (40) [show] [UniProt]


  1. Nasu, S., Wicks, F.D. and Gholson, R.K.
    L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.
    J. Biol. Chem. 257 : 626-632 (1982). [PMID: 7033218]
  2. Mortarino, M., Negri, A., Tedeschi, G., Simonic, T., Duga, S., Gassen, H.G. and Ronchi, S.
    L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.
    Eur. J. Biochem. 239 : 418-426 (1996). [PMID: 8706749]
  3. Tedeschi, G., Negri, A., Mortarino, M., Ceciliani, F., Simonic, T., Faotto, L. and Ronchi, S.
    L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity.
    Eur. J. Biochem. 239 : 427-433 (1996). [PMID: 8706750]
  4. Mattevi, A., Tedeschi, G., Bacchella, L., Coda, A., Negri, A. and Ronchi, S.
    Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family.
    Structure 7 : 745-756 (1999). [PMID: 10425677]
  5. Bossi, R. T., Negri, A., Tedeschi, G., Mattevi, A.
    Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis.
    Biochemistry 41 : 3018-3024 (2002). [PMID: 11863440]
  6. Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T.
    Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid.
    Plant Physiol. 141 : 851-857 (2006). [PMID: 16698895]

[EC created 1984, modified 2008]