|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 220.127.116.11
Enzymes and Genes:
|Arabidopsis thaliana col :||L-aspartate oxidase
|Escherichia coli K-12 substr. MG1655 :||L-aspartate oxidase
|Gossypium hirsutum :||L-aspartate oxidase
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
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
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -53.19825 [Latendresse13]
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]. 2-iminosuccinate can either be hydrolysed to form oxaloacetate and ammonia or can be used by EC 18.104.22.168, quinolinate synthase, in the production of quinolinate. The enzyme is a member of the succinate dehydrogenase/fumarate reductase family of enzymes [Bossi02].
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
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