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: Enzymatic synthesis;Galactokinase;Streptococcus pneumoniae;Substrate specificity
期刊名称:BIOORGANIC & MEDICINAL CHEMISTRY LETTERS ( 影响因子:2.823; 五年影响因子:2.677 )
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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.
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