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Eur J Biochem. 1991 Apr 23;197(2):373-9.

Purification and characterization of NADPH-dependent 2-oxoaldehyde reductase from porcine liver. A self-defence enzyme preventing the advanced stage of the Maillard reaction.

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Department of Agricultural Chemistry, University of Tokyo, Japan.


An enzyme which catalyzes the reduction of 3-deoxyglucosone to 3-deoxyfructose and methylglyoxal to acetol, was isolated and purified from porcine liver. 2-Oxoaldehyde compounds were found to be especially good substrates and monocarbonyl compounds were poor substrates for this reductase. The optimum pH of the enzyme activity was 6.5. The Km for 3-deoxyglucosone and methylglyoxal were 2.1 mM and 3.3 mM, respectively. The enzyme consisted of a single polypeptide chain with a molecular mass of 38 kDa. The activity of the enzyme was completely inhibited by p-chloromercuribenzoate. The enzyme inhibited the advanced stage of the Maillard reaction.

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