Substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4 towards galactose, glucose, and their derivatives
文献类型： 外文期刊
作者： Zou, Yang 3 ; Wang, Wenjun 1 ; Cai, Li; Chen, Leilei; Xue, Mengyang 3 ; Zhang, Xiaomei 3 ; Shen, Jie 1 ; Chen, Min 3 ;
作者机构： 1.Nankai Univ, Coll Pharm, Tianjin 300071, Peoples R China
2.Nankai Univ, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China
3.Shandong Univ, State Key Lab Microbial Technol, Natl Glycoengn Res Ctr, Jinan 250100, Shandong, Peoples R China
4.Shandong Univ, Dept Chem & Chem Engn, Jinan 250100, Shandong, Peoples R China
5.Shandong Univ, Dept Chem & Chem Engn, Jinan 250100, Shandong, Peoples
关键词： Galactokinase; Enzymatic synthesis; Substrate specificity; Streptococcus pneumoniae
期刊名称：BIOORGANIC & MEDICINAL CHEMISTRY LETTERS （ 影响因子：2.823； 五年影响因子：2.677 ）
ISSN： 0960-894X
年卷期： 2012 年 22 卷 10 期
页码：
收录情况： SCI
摘要： Galactokinases (GalKs) have attracted significant research attention for their potential applications in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 presents a remarkably broad substrate range including 14 diverse natural and unnatural sugars. TLC and MS studies revealed that GalKSpe4 had relaxed activity towards galactose derivatives with modifications on the C-6, 4- or 2-positions. Additionally, GalKSpe4 can also tolerate glucose while glucose derivatives with modifications on the C-6, 4- or 2-positions were unacceptable. More interestingly, GalKSpe4 can phosphorylate L-mannose in moderate yield (43%), while other L-sugars such as L-Gal cannot be recognized by this enzyme. These results are very significant because there is rarely enzyme reported that can phosphorylate such uncommon substrates as L-mannose. (C) 2012 Elsevier Ltd. All rights reserved.
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