Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12 |
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| Authors: | Junqiang Fang Wanyi Guan Li Cai Guofeng Gu Xianwei Liu Peng George Wang |
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| Affiliation: | aNational Glycoengineering Research Center and The State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong 250100, People’s Republic of China;bDepartments of Chemistry and Biochemistry, The Ohio State University, 484 W. 12th Ave., Columbus, OH 43210, USA |
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| Abstract: | N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Escherichia coli K12 is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. In this study, we report the broad substrate specificity of the pyrophosphorylase domain of GlmU during its uridyltransfer reaction and the substrate priority is ranked in the following order: UTP > dUTP > dTTP >> CTP > dATP/dm6 ATP. This pyrophosphorylase domain of GlmU is also a tool to synthesize UDP-GlcNAc analogs, two examples of which were synthesized herein in multiple mg scale in vitro. |
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| Keywords: | N-Acetylglucosamine-1-phosphate uridyltransferase Pyrophosphorylase domain Biosynthesis Substrate specificity |
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