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]
EC Number: 184.108.40.206L-aspartate + oxygen → 2-iminosuccinate + hydrogen peroxide + H+
The direction shown, i.e. which substrates are on the left and right sides, 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:
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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