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Characterization of aldehyde reductase of Sporobolomyces salmonicolor
M Kataoka1, H Sakai, T Morikawa
1Department of Agricultural Chemistry, Kyoto University, Japan.
Biochimica Et Biophysica Acta
|July 13, 1992
Abstract:
An NADPH-dependent aldehyde reductase (EC 1.1.1.2) isolated from Sporobolomyces salmonicolor AKU 4429 was further characterized. The enzyme also catalyzed the reductions of D-glucuronate, D-glucose, D-xylose and D-galactose at high concentrations. Km values for D-glucuronate and D-glucose are 345 and 4270 mM, respectively. Quercetin, dicoumarol and some SH-reagents inhibited the enzyme activity. NH2-terminal amino acid sequence analysis showed that the S. salmonicolor enzyme is partially the same as the aldo-keto reductase family proteins in primary protein structure.