A highly efficient galactokinase from Bifidobacterium infantis with broad substrate specificity
A highly efficient galactokinase from Bifidobacterium infantis with broad substrate specificity
复制标题
来自婴儿双歧杆菌的高效半乳糖激酶，具有广泛的底物特异性
DOI：
10.1016/j.carres.2012.04.022
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发表时间：
2012-07-01
影响因子：
3.1
通讯作者：
Wang, Peng
中科院分区：
文献类型：
--
作者：
Li, Lei;Liu, Yonghui;Wang, Peng
Galactokinase (GalK), particularly GalK from Escherichia coli, has been widely employed for the synthesis of sugar-1-phosphates. In this study, a GalK from Bifidobacterium infantis ATCC 15697 (BiGalK) was cloned and over-expressed with a yield of over 80 mg/L cell cultures. The k(cat)/K-m value of recombinant BiGalK toward galactose (164 s (1) mM (1) ) is 296 times higher than that of GalK from E. coli, indicating that BiGalK is much more efficient in the phosphorylation of galactose. The enzyme also exhibits activity toward galacturonic acid, which has never been observed on other wild type GalKs. Further activity assays showed that BiGalK has broad substrate specificity toward both sugars and phosphate donors. These features make BiGalK an attractive candidate for the large scale preparation of galactose-1-phosphate and derivatives. (C) 2012 Elsevier Ltd. All rights reserved.
