Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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 Wed Nov 26, 2014, biocyc13.