Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
twitter

MetaCyc Enzyme: L-aspartate oxidase
Inferred from experiment

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

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 → 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:
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 Pathway Tools version 19.5 (software by SRI International) on Mon Feb 8, 2016, biocyc12.