Kataoka M, Sakai H, Morikawa T, Katoh M, Miyoshi T, Shimizu S, Yamada H
Department of Agricultural Chemistry, Kyoto University, Japan.
Biochim Biophys Acta. 1992 Jul 13;1122(1):57-62. doi: 10.1016/0167-4838(92)90127-y.
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.
对从浅红酵母Sporobolomyces salmonicolor AKU 4429中分离出的一种NADPH依赖性醛还原酶（EC 1.1.1.2）进行了进一步表征。该酶在高浓度下还催化D-葡萄糖醛酸、D-葡萄糖、D-木糖和D-半乳糖的还原反应。D-葡萄糖醛酸和D-葡萄糖的Km值分别为345和4270 mM。槲皮素、双香豆素和一些巯基试剂抑制该酶的活性。氨基末端氨基酸序列分析表明，浅红酵母的这种酶在蛋白质一级结构上与醛酮还原酶家族蛋白部分相同。
