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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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MetaCyc Enzyme: methylglyoxal oxidase

Species: Pseudomonas putida

Summary:
methylglyoxal oxidase has been purified approximately 240 fold from Pseudomonas putida. The enzyme is specific for NAD (NADP is a potent inhibitor), and is active on 2-ketoaldehydes (methylglyoxal, glyoxal and methylglyoxal) and some aldehydes (see below) [Rhee87].

Similarly to the enzyme isolated from goat liver [Ray82], the enzyme is a monomer of 42 kDa, activated by fructose 1,6-bisphosphate, inhibited by NADP, and is most active at pH 8. However, the goat liver enzyme was not able to accpet aldehydes as substrates.

Molecular Weight of Polypeptide: 42 kD (experimental) [Rhee87 ]

Gene-Reaction Schematic: ?

Credits:
Created 31-Jan-2007 by Caspi R , SRI International


Enzymatic reaction of: methylglyoxal oxidase

methylglyoxal + NAD+ + H2O <=> pyruvate + NADH + 2 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 favored in the direction shown.

Alternative Substrates for methylglyoxal: propanal [Rhee87 ] , glycolaldehyde [Rhee87 ] , acetaldehyde [Rhee87 ] , formaldehyde [Rhee87 ] , phenylglyoxal [Rhee87 ] , glyoxal [Rhee87 ]

In Pathways: methylglyoxal degradation VII

Activators (Allosteric): Mg2+ [Rhee87] , fructose 1,6-bisphosphate [Rhee87]

Inhibitors (Allosteric): NADP+ [Rhee87]

Kinetic Parameters:

Substrate
Km (μM)
Citations
methylglyoxal
1000.0
[Rhee87]
NAD+
100.0
[Rhee87]

pH(opt): 8 [Rhee87]


References

Ray82: Ray S, Ray M (1982). "Purification and characterization of NAD and NADP-linked alpha-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate." J Biol Chem 257(18);10566-70. PMID: 7107625

Rhee87: Rhee, H.I., Watanabe, K., Murata, K., Kimura, A. (1987). "Metabolism of 2-oxoaldehyde in bacteria: oxidative conversion of methylglyoxal to pyruvate by an enzyme from Pseudomonas putida." Agric. Biol. Chem. 51: 1059-1066.


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 Dec 20, 2014, BIOCYC14B.