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 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.
In Pathways: methylglyoxal degradation VII
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.
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493