Substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4 towards galactose, glucose, and their derivatives

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• 作者：Yang Zou^a ; ^&dagger ; ; Wenjun Wang^b ; ^&dagger ; ; Li Cai^c ; Leilei Chen^d ; Mengyang Xue^a ; Xiaomei Zhang^a ; Jie Shen^b ; ^{jieshen@nankai.edu.cn} ; Min Chen^a ; ^{chenmin@sdu.edu.cn}
• 关键词：Galactokinase ; Enzymatic synthesis ; Substrate specificity ; Streptococcus pneumoniae
• 刊名：Bioorganic and Medicinal Chemistry Letters
• 出版年：2012
• 期刊代码：10_0960894x
• 类别：ch
• 出版时间：15 May, 2012
• 卷：22
• 期：10
• 页码：3540-3543
• 文件大小：2591 K

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.