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Functional characterization of an aldose reductase (bmALD1) obtained from the silkworm Bombyx mori.
Insect Molecular Biology ( IF 2.6 ) Pub Date : 2020-08-07 , DOI: 10.1111/imb.12658
K Yamamoto 1 , M Yamaguchi 1 , S Endo 2
Affiliation  

We describe a new member of the aldo‐keto reductase (AKR) superfamily in the silkworm Bombyx mori. On the basis of its amino acid sequence and phylogenetic tree, this AKR belongs to the AKR1B family and has been designated as bmALD1. In the current study, recombinant bmALD1 was overexpressed, purified to homogeneity and kinetically characterized. We discovered that bmALD1 uses NADPH as a coenzyme to reduce carbonyl compounds such as DL‐glyceraldehyde, glucose and 2‐nonenal. No NADH‐dependent activity was detected. To the best of our knowledge, bmALD1 is only the third AKR characterized in silkworm which, given its substrate specificity, could play a major role in glucose metabolism and antioxidant reactions. Our data provide an increased understanding of insect AKR function.

中文翻译:

从家蚕中获得的醛糖还原酶(bmALD1)的功能表征。

我们描述了家蚕Bombyx mori中aldo-keto还原酶(AKR)超家族的新成员。根据其氨基酸序列和系统发育树,该AKR属于AKR1B家族,已被命名为bmALD1。在当前的研究中,重组bmALD1被过表达,纯化至均一并进行了动力学表征。我们发现bmALD1使用NADPH作为辅酶来还原羰基化合物,例如DL-甘油醛,葡萄糖和2-壬烯醛。未检测到NADH依赖性活性。据我们所知,bmALD1只是家蚕中的第三个AKR,鉴于其底物特异性,它可能在葡萄糖代谢和抗氧化反应中起主要作用。我们的数据提供了对昆虫AKR功能的更多了解。
更新日期:2020-08-07
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