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Eur J Biochem. 1988 Jan 15;171(1-2):213-8.

Metabolism of 2-oxoaldehyde in mold. Purification and characterization of two methylglyoxal reductases from Aspergillus niger.

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1
Research Institute for Food Science, Kyoto University, Japan.

Abstract

Two kinds of methylglyoxal reductases were purified to apparent homogeneity from Aspergillus niger and designated MGR I and MGR II. Both enzymes consisted of a single polypeptide chain with a relative molecular mass of 36,000 (MGR I) and 38,000 (MGR II). NADPH was specifically required for the activities of both enzymes and Km values for NADPH were 54 microM (MGR I) and 6.8 microM (MGR II). MGR I was specific to 2-oxoaldehydes [glyoxal, methylglyoxal (Km = 15.4 mM) and phenylglyoxal], whereas MGR II was active on both 2-oxoaldehydes [glyoxal (Km = 10 mM), methylglyoxal (Km = 1.43 mM), phenylglyoxal (Km = 4.35 mM) and 4,5-dioxovalerate] and some aldehydes (propionaldehyde and acetaldehyde). Optimal pH values for MGR I and MGR II activities were 9.0 and 6.5 respectively. Both enzymes were inactivated by a brief incubation with 2-oxoaldehydes (glyoxal, methylglyoxal and phenylglyoxal) in the absence of NADPH. MGR I activity was competitively inhibited by NADP+ and the Ki value for NADP+ was calculated to be 0.49 mM. On the other hand, the inhibition of MGR II activity by NADP+ was of mixed type, the Ki value for NADP+ being 45 microM. MGR I was different from MGR II in amino acid composition.

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