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    Biochim Biophys Acta. 1992 Jul 13;1122(1):57-62.

    Characterization of aldehyde reductase of Sporobolomyces salmonicolor.

    Kataoka M, Sakai H, Morikawa T, Katoh M, Miyoshi T, Shimizu S, Yamada H.

    Department of Agricultural Chemistry, Kyoto University, Japan.

    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.

    PMID: 1633196 [PubMed - indexed for MEDLINE]

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