1.4.3.16: L-aspartate oxidase
This is an abbreviated version!
For detailed information about L-aspartate oxidase, go to the full flat file.
Word Map on EC 1.4.3.16
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1.4.3.16
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quinolinate
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nada
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fumarate
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pyridine
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flavoproteins
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iminoaspartate
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dihydroxyacetone
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flavoenzyme
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fad-binding
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biotechnology
- 1.4.3.16
- quinolinate
-
nada
- fumarate
- pyridine
- flavoproteins
- iminoaspartate
- dihydroxyacetone
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flavoenzyme
-
fad-binding
- biotechnology
Reaction
Synonyms
AO, At5g14760, FIN4, L-Asp oxidase, L-aspartate oxidase, LAO, LASPO, More, nadB, oxidase, L-aspartate, StLASPO, Tl-LASPO
ECTree
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General Information on EC 1.4.3.16 - L-aspartate oxidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
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although the enzyme mutation dramatically affects NADPH oxidase RBOHD function, it does not affect functions carried out by other members of the RBOH family, such as RBOHC and RBOHF
metabolism
physiological function
additional information
evolution
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NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate
evolution
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NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate
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metabolism
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the enzyme catalyzes the first irreversible step in the de novo biosynthesis of NAD+
physiological function
NadB and NadA (quinolinate synthase) interact with each other. The interaction is not species-specific and both proteins are not tightly bound to one another, indicating a function as a reversible multienzyme complex
physiological function
NadB shows three enzymatic activities: L-aspartate-oxygen oxidoreductase activity, fumarate reductase activity, and L-aspartate-fumarate oxidoreductase activity
physiological function
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LASPO is a flavoenzyme catalyzing the first step in the de novo biosynthesis of NAD+. The enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor
physiological function
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the enzyme is required for the reactive oxygen species burst mediated by the NADPH oxidase RBOHD triggered by the perception of several unrelated pathogen-associated molecular patterns. The enzyme is also required for RBOHD-dependent stomatal closure. The enzyme is required for stomatal immunity against the bacterium Pseudomonas syringa
physiological function
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the enzyme catalyzes a key metabolic step for the production of the nucleotide cofactor NAD+
additional information
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LASPO displays strong primary and tertiary structure similarity with the flavin containing subunit of the proteins belonging to the succinate dehydrogenase/fumarate reductase family. The similarity extends to the active site residues, with LASPO differing from the other enzymes of the family only for the presence of a conserved glutamate 121, which is substituted by apolar amino acids in the other enzymes
additional information
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full enzyme activity is not required for flg22-induced responses that are NADPH oxidase RBOHD-independent
