Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12.
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/dm(6) 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.
Fang
Junqiang
J
National Glycoengineering Research Center and The State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong 250100, People's Republic of China.
Guan
Wanyi
W
Cai
Li
L
Gu
Guofeng
G
Liu
Xianwei
X
Wang
Peng George
PG
D000117:Acetylglucosamine / Q000031:analogs & derivatives; D001665:Binding Sites; D048168:Escherichia coli K12 / Q000201:enzymology*; D015394:Molecular Structure; D009711:Nucleotides / Q000378:metabolism; D009713:Nucleotidyltransferases / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism; D011122:Polyphosphates / Q000378:metabolism*; D011487:Protein Conformation; D013379:Substrate Specificity; D014544:Uridine Triphosphate / Q000378:metabolism
D009711:Nucleotides; D010710:Phosphates; D011122:Polyphosphates; C026146:N-acetylglucosamine-1-phosphate; D009713:Nucleotidyltransferases; C023226:UDPacetylglucosamine pyrophosphorylase; C005692:triphosphoric acid; D014544:Uridine Triphosphate; D000117:Acetylglucosamine