Purification and characterization of NADPH‐dependent 2‐oxoaldehyde reductase from porcine liver
Open Access
- 1 April 1991
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 197 (2) , 373-379
- https://doi.org/10.1111/j.1432-1033.1991.tb15921.x
Abstract
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.Keywords
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