Document Detail

Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12.
MedLine Citation:
PMID:  19804974     Owner:  NLM     Status:  MEDLINE    
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.
Junqiang Fang; Wanyi Guan; Li Cai; Guofeng Gu; Xianwei Liu; Peng George Wang
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Publication Detail:
Type:  Journal Article     Date:  2009-09-17
Journal Detail:
Title:  Bioorganic & medicinal chemistry letters     Volume:  19     ISSN:  1464-3405     ISO Abbreviation:  Bioorg. Med. Chem. Lett.     Publication Date:  2009 Nov 
Date Detail:
Created Date:  2009-10-26     Completed Date:  2010-01-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9107377     Medline TA:  Bioorg Med Chem Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  6429-32     Citation Subset:  IM    
National Glycoengineering Research Center and The State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong 250100, People's Republic of China.
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MeSH Terms
Acetylglucosamine / analogs & derivatives
Binding Sites
Escherichia coli K12 / enzymology*
Molecular Structure
Nucleotides / metabolism
Nucleotidyltransferases / metabolism*
Phosphates / metabolism
Polyphosphates / metabolism*
Protein Conformation
Substrate Specificity
Uridine Triphosphate / metabolism
Reg. No./Substance:
0/Nucleotides; 0/Phosphates; 0/Polyphosphates; 10380-08-2/triphosphoric acid; 63-39-8/Uridine Triphosphate; 6866-69-9/N-acetylglucosamine-1-phosphate; 7512-17-6/Acetylglucosamine; EC 2.7.7.-/Nucleotidyltransferases; EC pyrophosphorylase

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