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MetaCyc Enzyme: L-aspartate oxidase

Species: Gossypium hirsutum

Summary:
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: ?

Credits:
Created 12-Oct-2006 by Foerster H , TAIR


Enzymatic reaction of: L-aspartate oxidase

EC Number: 1.4.3.16

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

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

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:

Substrate
Km (μM)
Citations
L-aspartate
660.0
[Hosokawa83]


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Jan 31, 2015, BIOCYC11A.