Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014

Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

Enzymes and Genes:
L-aspartate oxidase Inferred from experiment : nadB

In Pathway: NAD biosynthesis I (from aspartate)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: L-aspartate oxidase

Enzyme Commission Synonyms: NadB, Laspo, AO

First reaction in quinolinate biosynthesis, required for the de novo biosynthesis of NAD.

Enzyme Commission Summary:
A flavoprotein (FAD). L-Aspartate oxidase catalyses the first step in the de novo biosynthesis of NAD+ in some bacteria. oxygen can be replaced by fumarate as electron acceptor, yielding succinate [Bossi02]. The ability of the enzyme to use both O2 and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions [Bossi02]. α-iminosuccinate can either be hydrolysed to form oxaloacetate and ammonia 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 [Bossi02].

Citations: [Nasu82, Mortarino96, Tedeschi96, Mattevi99, Katoh06, Neidhardt96]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC:


Bossi02: Bossi RT, Negri A, Tedeschi G, Mattevi A (2002). "Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis." Biochemistry 41(9);3018-24. PMID: 11863440

Katoh06: Katoh A, Uenohara K, Akita M, Hashimoto T (2006). "Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid." Plant Physiol 141(3);851-7. PMID: 16698895

Mattevi99: Mattevi A, Tedeschi G, Bacchella L, Coda A, Negri A, Ronchi S (1999). "Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family." Structure Fold Des 7(7);745-56. PMID: 10425677

Mortarino96: Mortarino M, Negri A, Tedeschi G, Simonic T, Duga S, Gassen HG, Ronchi S (1996). "L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition." Eur J Biochem 239(2);418-26. PMID: 8706749

Nasu82: Nasu S, Wicks FD, Gholson RK (1982). "L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase." J Biol Chem 1982;257(2);626-32. PMID: 7033218

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

Tedeschi96: Tedeschi G, Negri A, Mortarino M, Ceciliani F, Simonic T, Faotto L, Ronchi S (1996). "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(2);427-33. PMID: 8706750

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, biocyc14.