EC 1 - Oxidoreductases
EC 1.4 - Acting on the CH-NH2 group of donors
EC 1.4.3 - With oxygen as acceptor
EC 1.4.3.16 - L-aspartate oxidase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.4.3.16
Names
Accepted name:
L-aspartate oxidase
Other
names:
NadB
Laspo
AO
LASPO
Laspo
AO
LASPO
Systematic name:
L-aspartate:oxygen oxidoreductase (deaminating)
Reaction
- L-aspartate + O2 = iminosuccinate + H2O2
Cofactor
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
Gene Ontology:
GO:0008734
,
GO:0044318
CAS Registry Number:
69106-47-4
References
-
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]
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L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.Eur. J. Biochem. 239 : 418-426 (1996). [PMID: 8706749]
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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]
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Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family.Structure 7 : 745-756 (1999). [PMID: 10425677]
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Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis.Biochemistry 41 : 3018-3024 (2002). [PMID: 11863440]
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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]