人源 UDP-N-乙酰氨基半乳糖胺焦磷酸化酶（AGX1）的核苷酸三磷酸底物特异性研究。
Investigation of the nucleotide triphosphate substrate specificity of Homo sapiens UDP-N-acetylgalactosamine pyrophosphorylase (AGX1).
机构信息
National Glycoengineering Research Center, Jinan, Shandong 250100, People's Republic of China.
出版信息
Bioorg Med Chem Lett. 2012 Jun 15;22(12):3957-61. doi: 10.1016/j.bmcl.2012.04.102. Epub 2012 Apr 28.
Nucleotide sugars are essential glycosyl donors for Leloir-type glycosyltransferases. The UDP-N-acetylgalactosamine pyrophosphorylase (UDP-GalNAc PP; AGX1) from Homo sapiens catalyzes the synthesis of UDP-N-acetylgalactosamine from N-acetylgalactosamine 1-phosphate and UTP. In this Letter, we systematically studied nucleotide substrate specificity of AGX1 during its uridyltransfer reaction, and described the capability of AGX1 to catalyze dUTP and dTTP to their corresponding nucleotide sugars for the first time. Furthermore, using such a eukaryotic enzyme, we synthesized dUDP-GalNAc and dTDP-GalNAc in multiple mg scale in vitro efficiently and rapidly.
核苷酸糖是 Leloir 型糖基转移酶的必需糖基供体。人源 UDP-N-乙酰半乳糖胺焦磷酸化酶（UDP-GalNAc PP；AGX1）可催化 N-乙酰半乳糖胺 1-磷酸和 UTP 合成 UDP-N-乙酰半乳糖胺。在本研究中，我们系统地研究了 AGX1 在其尿苷酰转移反应过程中的核苷酸底物特异性，并首次描述了 AGX1 催化 dUTP 和 dTTP 生成相应核苷酸糖的能力。此外，我们还利用这种真核酶在体外高效快速地合成了毫克级别的 dUDP-GalNAc 和 dTDP-GalNAc。
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