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. 1992 Jul 13;1122(1):57-62.
doi: 10.1016/0167-4838(92)90127-y.

Characterization of aldehyde reductase of Sporobolomyces salmonicolor

M Kataoka  1 , H Sakai, T Morikawa, M Katoh, T Miyoshi, S Shimizu, H Yamada
Affiliations

Characterization of aldehyde reductase of Sporobolomyces salmonicolor

M Kataoka et al. Biochim Biophys Acta. .

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.

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