Purification and characterization of NADPH-dependent 2-oxoaldehyde reductase from porcine liver. A self-defence enzyme preventing the advanced stage of the Maillard reaction.
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.
Liang
Z Q
ZQ
Department of Agricultural Chemistry, University of Tokyo, Japan.
Hayase
F
F
Kato
H
H
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D015416:Maillard Reaction; D013552:Swine
D000596:Amino Acids; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+)