MetaCyc Enzyme: methylglyoxal oxidase

Species: Pseudomonas putida

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

Gene-Reaction Schematic

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

Enzymatic reaction of: methylglyoxal oxidase

Inferred from experiment

methylglyoxal + NAD+ + H2O → pyruvate + NADH + 2 H+

The direction shown, i.e. which substrates are on the left and right sides, 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]


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 Pathway Tools version 19.5 (software by SRI International) on Sat Nov 28, 2015, biocyc13.