MetaCyc Enzyme: L-aspartate oxidase

Species: Gossypium hirsutum

L-aspartate oxidase was partially purified from callus tissues of Gossypium hirsutum. The enzyme expressed high specificity towards L-aspartate and did not accept L-glutamate, D-aspartate or D- or L-alanine [Hosokawa83].

Molecular Weight of Polypeptide: 83 kD (experimental) [Hosokawa83 ]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Created 12-Oct-2006 by Foerster H , TAIR

Enzymatic reaction of: L-aspartate oxidase

EC Number:

L-aspartate + oxygen <=> 2-iminosuccinate + hydrogen peroxide + H+

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.

The reaction is physiologically favored in the direction shown.

In Pathways: NAD biosynthesis I (from aspartate)

Inhibitors (Unknown Mechanism): NAD+ [Hosokawa83]

Primary Physiological Regulators of Enzyme Activity: NAD+

Kinetic Parameters:

Km (μM)


Hosokawa83: Hosokawa Y, Mitchell E, Gholson RK (1983). "Higher plants contain L-asparate oxidase, the first enzyme of the Escherichia coli quinolinate synthetase system." Biochem Biophys Res Commun 111(1);188-93. PMID: 6338879

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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