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: 188.8.131.52
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)
Primary Physiological Regulators of Enzyme Activity: NAD+
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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