Compounds > uridine diphosphate n-acetylglucosamine
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uridine diphosphate n-acetylglucosamine and phosphoenolpyruvate

uridine diphosphate n-acetylglucosamine has been researched along with phosphoenolpyruvate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19902 (50.00)18.7374
1990's1 (25.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Anwar, RA; Zemell, RI1
Anwar, RA; Vlaovic, M1
Benson, TE; Filman, DJ; Hogle, JM; Walsh, CT1
Amrhein, N; Etezady-Esfarjani, T; Macheroux, P; Samland, AK1

Other Studies

4 other study(ies) available for uridine diphosphate n-acetylglucosamine and phosphoenolpyruvate

ArticleYear
Mechanism of pyruvate-uridine diphospho-N-acetylglucosamine transferase. Evidence for an enzyme-enolpyruvate intermediate.
    The Journal of biological chemistry, 1975, Jul-10, Volume: 250, Issue:13

    Topics: Butyrates; Carbon Radioisotopes; Deuterium; Enterobacteriaceae; Phosphoenolpyruvate; Phosphorus Radioisotopes; Transferases; Tritium; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate Sugars

1975
Effect of phosphoenolpyruvate analogs on the activity of enoylpyruvate transferase and the effect of UDP-N-acetylglucosamine on the reactivity of the active site SH group.
    Biochimica et biophysica acta, 1980, Dec-04, Volume: 616, Issue:2

    Topics: Alkyl and Aryl Transferases; Binding Sites; In Vitro Techniques; Iodoacetates; Phosphoenolpyruvate; Pyruvate Kinase; Sulfhydryl Compounds; Transferases; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate Sugars

1980
An enzyme-substrate complex involved in bacterial cell wall biosynthesis.
    Nature structural biology, 1995, Volume: 2, Issue:8

    Topics: Amino Acid Sequence; Anti-Infective Agents; Binding Sites; Carbohydrate Dehydrogenases; Cell Wall; Computer Graphics; Computer Simulation; Crystallography, X-Ray; Drug Design; Flavin-Adenine Dinucleotide; Hydrogen Bonding; Ligands; Models, Molecular; Models, Structural; Molecular Sequence Data; Phosphoenolpyruvate; Protein Structure, Secondary; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate N-Acetylmuramic Acid

1995
Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae.
    Biochemistry, 2001, Feb-13, Volume: 40, Issue:6

    Topics: Alkyl and Aryl Transferases; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Cysteine; Enterobacter cloacae; Enzyme Inhibitors; Fosfomycin; Mutagenesis, Site-Directed; Phosphates; Phosphoenolpyruvate; Recombinant Proteins; Uridine Diphosphate N-Acetylglucosamine

2001