Compounds > n-acetylglucosamine-1-phosphate

n-acetylglucosamine-1-phosphate and triphosphoric-acid

n-acetylglucosamine-1-phosphate has been researched along with triphosphoric-acid* in 1 studies

Other Studies

1 other study(ies) available for n-acetylglucosamine-1-phosphate and triphosphoric-acid

Article	Year
Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12. Bioorganic & medicinal chemistry letters, 2009, Nov-15, Volume: 19, Issue:22 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. Topics: Acetylglucosamine; Binding Sites; Escherichia coli K12; Molecular Structure; Nucleotides; Nucleotidyltransferases; Phosphates; Polyphosphates; Protein Conformation; Substrate Specificity; Uridine Triphosphate	2009

Article

Year

Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12.

Bioorganic & medicinal chemistry letters, 2009, Nov-15, Volume: 19, Issue:22

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.

Topics: Acetylglucosamine; Binding Sites; Escherichia coli K12; Molecular Structure; Nucleotides; Nucleotidyltransferases; Phosphates; Polyphosphates; Protein Conformation; Substrate Specificity; Uridine Triphosphate

2009