IntEnz

EC 1.4.3.16 - L-aspartate oxidase

IntEnz Enzyme Nomenclature
EC 1.4.3.16

Names

Reaction

• 25876 [IUBMB]
  L-aspartate

  L-aspartate

  Name origin: UniProt - CHECKED (C)

  CHEBI:29991

  Formula: C4H6NO4
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  O₂

  O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:15379

  Formula: O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  H₂O₂

  H2O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:16240

  Formula: H2O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  iminosuccinate

  iminosuccinate

  Name origin: UniProt - CHECKED (C)

  CHEBI:77875

  Formula: C4H4NO4
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

Cofactor

• FAD

Comments:

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 2.5.1.72, 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

References

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 1.4.3.16 created 1984, modified 2008]