MetaCyc Enzyme: methylglyoxal reductase (NADPH-dependent)

Species: Escherichia coli K-12 substr. MG1655

Methylglyoxal reductase catalyzes the conversion of methylglyoxal into lactaldehyde. The lactaldehyde is then acted upon by lactaldehyde dehydrogenase yielding lactate. This provides an alternate route for methylglyoxal metabolism [Saikusa87]. No gene has been identified for this enzyme.

Molecular Weight of Polypeptide: 43.0 kD (experimental) [Saikusa87 ]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Enzymatic reaction of: methylglyoxal reductase (NADPH-dependent)

EC Number:

(S)-lactaldehyde + NADP+ <=> methylglyoxal + NADPH + 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 opposite direction.

Alternative Substrates for methylglyoxal [Saikusa87 ]: glycolaldehyde [Saikusa87 ] , acetaldehyde [Saikusa87 ] , propanal [Saikusa87 ] , DL-glyceraldehyde [Saikusa87 ] , 4,5-dioxopentanoate [Saikusa87 ] , phenylglyoxal [Saikusa87 ] , glyoxal [Saikusa87 ]

Alternative Substrates for NADPH [Saikusa87 ]: NADH

In Pathways: superpathway of methylglyoxal degradation , methylglyoxal degradation IV

Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

The enzyme was purified from E. coli IFO 3806 [Saikusa87].

Activators (Unknown Mechanism): glutathione [Saikusa87] , L-dithiothreitol [Saikusa87] , 2-mercaptoethanol [Saikusa87]

Inhibitors (Unknown Mechanism): Cu2+ [Saikusa87] , Zn2+ [Saikusa87] , Ni2+ [Saikusa87] , Co2+ [Saikusa87] , p-chloromercuribenzoate [Saikusa87]

Primary Physiological Regulators of Enzyme Activity: Cu2+ , Zn2+ , Ni2+ , Co2+

Kinetic Parameters:

Km (μM)

T(opt): 45 °C [Saikusa87]

pH(opt): 6.5 [Saikusa87]


Saikusa87: Saikusa T, Rhee H, Watanabe K, Murata K, Kimura A (1987). "Metabolism of 2-oxoaldehydes in bacteria: purification and characterization of methylglyoxal reductase from E. coli." Agricultural and Biological Chemistry 51(7): 1893-1899.

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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
Page generated by SRI International Pathway Tools version 19.0 on Sun Oct 4, 2015, BIOCYC14B.