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) [Rhee87a].
Similarly to the enzyme isolated from goat liver [Ray82a], 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) [Rhee87a ]
Enzymatic reaction of: methylglyoxal oxidase
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 [Rhee87a], glycolaldehyde [Rhee87a], acetaldehyde [Rhee87a], formaldehyde [Rhee87a], phenylglyoxal [Rhee87a], glyoxal [Rhee87a]
In Pathways: methylglyoxal degradation VIIActivators (Allosteric): Mg2+ [Rhee87a], fructose 1,6-bisphosphate [Rhee87a] Inhibitors (Allosteric): NADP+ [Rhee87a]Kinetic Parameters:
pH(opt): 8 [Rhee87a]
Ray82a: 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
Rhee87a: 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.
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