Page last updated: 2024-09-03

glucosamine 6-phosphate and acetyl coenzyme a

glucosamine 6-phosphate has been researched along with acetyl coenzyme a in 4 studies

Compound Research Comparison

Studies
(glucosamine 6-phosphate)
Trials
(glucosamine 6-phosphate)
Recent Studies (post-2010)
(glucosamine 6-phosphate)
Studies
(acetyl coenzyme a)
Trials
(acetyl coenzyme a)
Recent Studies (post-2010) (acetyl coenzyme a)
1240473,551141,291

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (25.00)18.2507
2000's1 (25.00)29.6817
2010's2 (50.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Jaberi-Pour, M; Vessal, M1
Li, LF; Liang, YH; Liu, X; Su, XD; Wang, J1
Chaubey, A; Chib, R; Jamwal, U; Khan, IA; Lambu, MR; Mukherjee, D; Rani, C; Sharma, R; Wazir, P1
Allingham, JS; Anastassiades, T; Brockhausen, I; Chen, M; Nair, DG; Szarek, WA; Yang, X1

Other Studies

4 other study(ies) available for glucosamine 6-phosphate and acetyl coenzyme a

ArticleYear
Partial purification and kinetic properties of three different D-glucosamine 6-P:N-acetyltransferase forms from human placenta.
    Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 1998, Volume: 121, Issue:4

    Topics: Acetyl Coenzyme A; Acetyltransferases; Animals; Dithiothreitol; Enzyme Inhibitors; Female; Glucosamine; Glucosamine 6-Phosphate N-Acetyltransferase; Glucose-6-Phosphate; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Isoenzymes; Kinetics; p-Chloromercuribenzoic Acid; Placenta; Pregnancy; Species Specificity; Substrate Specificity; Sulfhydryl Reagents

1998
Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1.
    FEBS letters, 2008, Sep-03, Volume: 582, Issue:20

    Topics: Acetyl Coenzyme A; Alanine; Apoenzymes; Crystallography, X-Ray; Glucosamine; Glucosamine 6-Phosphate N-Acetyltransferase; Glucose-6-Phosphate; Glutamic Acid; Humans; Mutagenesis

2008
Escherichia coli N-Acetylglucosamine-1-Phosphate-Uridyltransferase/Glucosamine-1-Phosphate-Acetyltransferase (GlmU) Inhibitory Activity of Terreic Acid Isolated from Aspergillus terreus.
    Journal of biomolecular screening, 2016, Volume: 21, Issue:4

    Topics: Acetyl Coenzyme A; Animals; Anti-Bacterial Agents; Aspergillus; Binding, Competitive; Biofilms; Biological Assay; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Gene Expression; Glucosamine; Glucose-6-Phosphate; Microbial Sensitivity Tests; Microsomes, Liver; Molecular Docking Simulation; Multienzyme Complexes; Mutation; Protein Binding; Protein Domains; Quinones; Rats; Secondary Metabolism

2016
Human acetyl-CoA:glucosamine-6-phosphate N-acetyltransferase 1 has a relaxed donor specificity and transfers acyl groups up to four carbons in length.
    Biochemistry and cell biology = Biochimie et biologie cellulaire, 2016, Volume: 94, Issue:2

    Topics: Acetyl Coenzyme A; Carbon; Fluorescence; Glucosamine; Glucosamine 6-Phosphate N-Acetyltransferase; Glucose-6-Phosphate; Humans; Spectrophotometry

2016