MetaCyc Enzyme: methylglyoxal reductase (NADH-dependent)

Species: Rattus norvegicus

An enzyme has been partially purified from rat liver that oxidizes (R)-lactaldehyde to methylglyoxal using NAD+ as the elctrons acceptor [Ting65]. The enzyme is specific to the D-isomer of lactaldehyde and to NADH, and catalyzes a reversible reaction. Enzymatic activity was found in all tissues tested (muscle, brain, kidney, heart, liver, spleen, lung), but was strongest in skeletal muscle and weakest in lung.

This mammalian enzyme differs from methylglyoxal reductase (NADPH-dependent) (EC in using NADH rather than NADPH. In addition, catalyzes a unidirectional reduction of methylglyoxal to (R)-lactaldehyde, while the mammalian enzyme catalyzes a reversible reaction.

Gene-Reaction Schematic

Gene-Reaction Schematic

Created 16-Jan-2007 by Caspi R, SRI International

Enzymatic reaction of: methylglyoxal reductase (NADH-dependent)

Inferred from experiment

EC Number:

(R)-lactaldehyde + NAD+ ⇄ methylglyoxal + NADH + H+

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates for (R)-lactaldehyde: D-glyceraldehyde [Ting65]

In Pathways: methylglyoxal degradation VI

Inhibitors (Other): p-chloromercuribenzoate [Ting65], iodoacetate [Ting65], N-ethylmaleimide [Ting65]Kinetic Parameters:
Substrate Km (μM) Citations
NAD+ 34.0 [Ting65]
(R)-lactaldehyde 130.0 [Ting65]

pH(opt): 11 [Ting65]


Ting65: Ting, S.M., Miller, O.N., Sellinger, O.Z. (1965). "The metabolism of lactaldehyde. VII. The oxidation of D-lactaldehyde in rat liver." Biochim Biophys Acta 97;407-15. PMID: 14323585

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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